|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5353 |
| Enzyme 1 Name |
Succinate dehydrogenase cytochrome b560 subunit, mitochondrial |
| Enzyme 1 Synonyms |
- Integral membrane protein CII-3
- QPs-1
- QPs1
- Succinate dehydrogenase complex subunit C
- Succinate-ubiquinone oxidoreductase cytochrome B large subunit
- CYBL
|
| Enzyme 1 Gene Name |
SDHC |
| Enzyme 1 Protein Sequence |
>Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYS
WSLPMAMSICHRGTGIALSAGVSLFGMSALLLPGNFESYLELVKSLCLGPALIHTAKFAL
VFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVVVLVLTVLSSMGLAAM
|
| Enzyme 1 Number of Residues |
169 |
| Enzyme 1 Molecular Weight |
18610.0 |
| Enzyme 1 Theoretical pI |
10.12 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- electron carrier activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- succinate dehydrogenase activity
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- tricarboxylic acid cycle
|
| Component |
- cell part
- membrane
- membrane part
- plasma membrane part
- plasma membrane succinate dehydrogenase complex
|
|
| Enzyme 1 General Function |
Involved in succinate dehydrogenase activity |
| Enzyme 1 Specific Function |
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) |
| Enzyme 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
Not Available |
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q99643  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
C560_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>510 bp
ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATGCTGTTCCTTTGGGAACCACGGCCAAAGAAGAGATGGAGCGG
TTCTGGAATAAGAATATAGGTTCAAACCGTCCTCTGTCTCCCCACATTACTATCTACAGT
TGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACTGGTATTGCTTTGAGTGCA
GGGGTCTCTCTTTTTGGCATGTCGGCCCTGTTACTCCCTGGGAACTTTGAGTCTTATTTG
GAACTTGTGAAGTCCCTGTGTCTGGGGCCAGCACTGATCCACACAGCTAAGTTTGCACTT
GTCTTCCCTCTCATGTATCATACCTGGAATGGGATCCGACACTTGATGTGGGACCTAGGA
AAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTTGTCCTGGTTCTTACTGTG
TTGTCCTCTATGGGGCTGGCAGCCATGTGA
|
| Enzyme 1 GenBank Gene ID |
U57877  |
| Enzyme 1 GeneCard ID |
SDHC  |
| Enzyme 1 GenAtlas ID |
SDHC  |
| Enzyme 1 HGNC ID |
HGNC:10682  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1q23.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K: Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. Cytogenet Cell Genet. 1997;79(1-2):132-8. [PubMed
]
- Elbehti-Green A, Au HC, Mascarello JT, Ream-Robinson D, Scheffler IE: Characterization of the human SDHC gene encoding of the integral membrane proteins of succinate-quinone oxidoreductase in mitochondria. Gene. 1998 Jun 15;213(1-2):133-40. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Niemann S, Muller U: Mutations in SDHC cause autosomal dominant paraganglioma, type 3. Nat Genet. 2000 Nov;26(3):268-70. [PubMed
]
- McWhinney SR, Pasini B, Stratakis CA: Familial gastrointestinal stromal tumors and germ-line mutations. N Engl J Med. 2007 Sep 6;357(10):1054-6. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5382 |
| Enzyme 2 Name |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial |
| Enzyme 2 Synonyms |
- Flavoprotein subunit of complex II
- Fp
|
| Enzyme 2 Gene Name |
SDHA |
| Enzyme 2 Protein Sequence |
>Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
MSGVRGLSRLLSARRLALAKAWPTVLQTGTRGFHFTVDGNKRASAKVSDSISAQYPVVDH
EFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWR
WHFYDTVKGSDWLGDQDAIHYMTEQAPAAVVELENYGMPFSRTEDGKIYQRAFGGQSLKF
GKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIE
DGSIHRIRAKNTVVATGGYGRTYFSCTSAHTSTGDGTAMITRAGLPCQDLEFVQFHPTGI
YGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPE
KDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQ
VLRHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIEESCRPGDK
VPPIKPNAGEESVMNLDKLRFADGSIRTSELRLSMQKSMQNHAAVFRVGSVLQEGCGKIS
KLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVR
IDEYDYSKPIQGQQKKPFEEHWRKHTLSYVDVGTGKVTLEYRPVIDKTLNEADCATVPPA
IRSY
|
| Enzyme 2 Number of Residues |
664 |
| Enzyme 2 Molecular Weight |
72691.0 |
| Enzyme 2 Theoretical pI |
7.41 |
| Enzyme 2 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- electron carrier activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- purine nucleoside binding
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- electron transport chain
- generation of precursor metabolites and energy
- metabolic process
- oxidation reduction
- tricarboxylic acid cycle
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in electron carrier activity |
| Enzyme 2 Specific Function |
Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- succinate + ubiquinone = fumarate + ubiquinol [RN:R02164]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P31040  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
DHSA_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1995 bp
ATGTCGGGGGTCCGGGGCCTGTCGCGGCTGCTGAGCGCTCGGCGCCTGGCGCTGGCCAAG
GCGTGGCCAACAGTGTTGCAAACAGGAACCCGAGGTTTTCACTTCACTGTTGATGGGAAC
AAGAGGGCATCTGCTAAAGTTTCAGATTCCATTTCTGCTCAGTATCCAGTAGTGGATCAT
GAATTTGATGCAGTGGTGGTAGGCGCTGGAGGGGCAGGCTTGCGAGCTGCATTTGGCCTT
TCTGAGGCAGGGTTTAATACAGCATGTGTTACCAAGCTGTTTCCTACCAGGTCACACACT
GTTGCAGCACAGGGAGGAATCAATGCTGCTCTGGGGAACATGGAGGAGGACAACTGGAGG
TGGCATTTCTACGACACCGTGAAGGGCTCCGACTGGCTGGGGGACCAGGATGCCATCCAC
TACATGACGGAGCAGGCCCCCGCCGCCGTGGTCGAGCTAGAAAATTATGGCATGCCGTTT
AGCAGAACTGAAGATGGGAAGATTTATCAGCGTGCATTTGGTGGACAGAGCCTCAAGTTT
GGAAAGGGCGGGCAGGCCCATCGGTGCTGCTGTGTGGCTGATCGGACTGGCCACTCGCTA
TTGCACACCTTATATGGACGGTCTCTGCGATATGATACCAGCTATTTTGTGGAGTATTTT
GCCTTGGATCTCCTGATGGAGAACGGGGAGTGCCGTGGTGTCATCGCACTGTGCATAGAG
GACGGGTCCATCCATCGCATAAGAGCAAAGAACACTGTTGTTGCCACAGGAGGCTACGGG
CGCACCTACTTCAGCTGCACGTCTGCCCACACCAGCACTGGCGACGGCACGGCCATGATC
ACCAGGGCAGGCCTTCCTTGCCAGGACCTAGAGTTTGTTCAGTTCCACCCTACAGGCATA
TATGGTGCTGGTTGTCTCATTACGGAAGGATGTCGTGGAGAGGGAGGCATTCTCATTAAC
AGTCAAGGCGAAAGGTTTATGGAGCGATACGCCCCTGTCGCGAAGGACCTGGCGTCTAGA
GATGTGGTGTCTCGGTCCATGACTCTGGAGATCCGAGAAGGAAGAGGCTGTGGCCCTGAG
AAAGATCACGTCTACCTGCAGCTGCACCACCTACCTCCAGAGCAGCTGGCCACGCGCCTG
CCTGGCATTTCAGAGACAGCCATGATCTTCGCTGGCGTGGACGTCACGAAGGAGCCGATC
CCTGTCCTCCCCACCGTGCATTATAACATGGGCGGCATTCCCACCAACTACAAGGGGCAG
GTCCTGAGGCACGTGAATGGCCAGGATCAGATTGTGCCCGGCCTGTACGCCTGTGGGGAG
GCCGCCTGTGCCTCGGTACATGGTGCCAACCGCCTCGGGGCAAACTCGCTCTTGGACCTG
GTTGTCTTTGGTCGGGCATGTGCCCTGAGCATCGAAGAGTCATGCAGGCCTGGAGATAAA
GTCCCTCCAATTAAACCAAACGCTGGGGAAGAATCTGTCATGAATCTTGACAAATTGAGA
TTTGCTGATGGAAGCATAAGAACATCGGAACTGCGACTCAGCATGCAGAAGTCAATGCAA
AATCATGCTGCCGTGTTCCGTGTGGGAAGCGTGTTGCAAGAAGGTTGTGGGAAAATCAGC
AAGCTCTATGGAGACCTAAAGCACCTGAAGACGTTCGACCGGGGAATGGTCTGGAACACG
GACCTGGTGGAGACCCTGGAGCTGCAGAACCTGATGCTGTGTGCGCTGCAGACCATCTAC
GGAGCAGAGGCACGGAAGGAGTCACGGGGCGCGCATGCCAGGGAAGACTACAAGGTGCGG
ATTGATGAGTACGATTACTCCAAGCCCATCCAGGGGCAACAGAAGAAGCCCTTTGAGGAG
CACTGGAGGAAGCACACCCTGTCCTATGTGGACGTTGGCACTGGGAAGGTCACTCTGGAA
TATAGACCCGTGATCGACAAAACTTTGAACGAGGCTGACTGTGCCACCGTCCCGCCAGCC
ATTCGCTCCTACTGA
|
| Enzyme 2 GenBank Gene ID |
D30648  |
| Enzyme 2 GeneCard ID |
SDHA  |
| Enzyme 2 GenAtlas ID |
SDHA  |
| Enzyme 2 HGNC ID |
HGNC:10680  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5p15 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hirawake H, Wang H, Kuramochi T, Kojima S, Kita K: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria. J Biochem (Tokyo). 1994 Jul;116(1):221-7. [PubMed
]
- Morris AA, Farnsworth L, Ackrell BA, Turnbull DM, Birch-Machin MA: The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase. Biochim Biophys Acta. 1994 Mar 29;1185(1):125-8. [PubMed
]
- Parfait B, Chretien D, Rotig A, Marsac C, Munnich A, Rustin P: Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome. Hum Genet. 2000 Feb;106(2):236-43. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-Pequignot E, Munnich A, Rotig A: Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet. 1995 Oct;11(2):144-9. [PubMed
]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed
]
- Hao HX, Khalimonchuk O, Schraders M, Dephoure N, Bayley JP, Kunst H, Devilee P, Cremers CW, Schiffman JD, Bentz BG, Gygi SP, Winge DR, Kremer H, Rutter J: SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma. Science. 2009 Aug 28;325(5944):1139-42. Epub 2009 Jul 23. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Van Coster R, Seneca S, Smet J, Van Hecke R, Gerlo E, Devreese B, Van Beeumen J, Leroy JG, De Meirleir L, Lissens W: Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II. Am J Med Genet A. 2003 Jul 1;120(1):13-8. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5411 |
| Enzyme 3 Name |
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial |
| Enzyme 3 Synonyms |
- CybS
- CII-4
- QPs3
- Succinate dehydrogenase complex subunit D
- Succinate-ubiquinone oxidoreductase cytochrome b small subunit
- Succinate-ubiquinone reductase membrane anchor subunit
|
| Enzyme 3 Gene Name |
SDHD |
| Enzyme 3 Protein Sequence |
>Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSK
AASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDAL
QKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL
|
| Enzyme 3 Number of Residues |
159 |
| Enzyme 3 Molecular Weight |
17042.8 |
| Enzyme 3 Theoretical pI |
8.75 |
| Enzyme 3 GO Classification |
| Function |
- binding
- cation binding
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- transition metal ion binding
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- tricarboxylic acid cycle
|
| Component |
- cell part
- envelope
- integral to membrane
- intrinsic to membrane
- membrane part
- mitochondrial envelope
- organelle envelope
|
|
| Enzyme 3 General Function |
Involved in iron ion binding |
| Enzyme 3 Specific Function |
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O14521  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
DHSD_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>480 bp
ATGGCGGTTCTCTGGAGGCTGAGTGCCGTTTGCGGTGCCCTAGGAGGCCGAGCTCTGTTG
CTTCGAACTCCAGTGGTCAGACCTGCTCATATCTCAGCATTTCTTCAGGACCGACCTATC
CCAGAATGGTGTGGAGTGCAGCACATACACTTGTCACCGAGCCACCATTCTGGCTCCAAG
GCTGCATCTCTCCACTGGACTAGCGAGAGGGTTGTCAGTGTTTTGCTCCTGGGTCTGCTT
CCGGCTGCTTATTTGAATCCTTGCTCTGCGATGGACTATTCCCTGGCTGCAGCCCTCACT
CTTCATGGTCACTGGGGCCTTGGACAAGTTGTTACTGACTATGTTCATGGGGATGCCTTG
CAGAAAGCTGCCAAGGCAGGGCTTTTGGCACTTTCAGCTTTAACCTTTGCTGGGCTTTGC
TATTTCAACTATCACGATGTGGGCATCTGCAAAGCTGTTGCCATGCTGTGGAAGCTCTGA
|
| Enzyme 3 GenBank Gene ID |
AB006202  |
| Enzyme 3 GeneCard ID |
SDHD  |
| Enzyme 3 GenAtlas ID |
SDHD  |
| Enzyme 3 HGNC ID |
HGNC:10683  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
11q23 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K: Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. Cytogenet Cell Genet. 1997;79(1-2):132-8. [PubMed
]
- Hirawake H, Taniwaki M, Tamura A, Amino H, Tomitsuka E, Kita K: Characterization of the human SDHD gene encoding the small subunit of cytochrome b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase. Biochim Biophys Acta. 1999 Aug 4;1412(3):295-300. [PubMed
]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gimm O, Armanios M, Dziema H, Neumann HP, Eng C: Somatic and occult germ-line mutations in SDHD, a mitochondrial complex II gene, in nonfamilial pheochromocytoma. Cancer Res. 2000 Dec 15;60(24):6822-5. [PubMed
]
- Baysal BE, Ferrell RE, Willett-Brozick JE, Lawrence EC, Myssiorek D, Bosch A, van der Mey A, Taschner PE, Rubinstein WS, Myers EN, Richard CW 3rd, Cornelisse CJ, Devilee P, Devlin B: Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma. Science. 2000 Feb 4;287(5454):848-51. [PubMed
]
- Milunsky JM, Maher TA, Michels VV, Milunsky A: Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma. Am J Med Genet. 2001 May 15;100(4):311-4. [PubMed
]
- Badenhop RF, Cherian S, Lord RS, Baysal BE, Taschner PE, Schofield PR: Novel mutations in the SDHD gene in pedigrees with familial carotid body paraganglioma and sensorineural hearing loss. Genes Chromosomes Cancer. 2001 Jul;31(3):255-63. [PubMed
]
- Taschner PE, Jansen JC, Baysal BE, Bosch A, Rosenberg EH, Brocker-Vriends AH, van Der Mey AG, van Ommen GJ, Cornelisse CJ, Devilee P: Nearly all hereditary paragangliomas in the Netherlands are caused by two founder mutations in the SDHD gene. Genes Chromosomes Cancer. 2001 Jul;31(3):274-81. [PubMed
]
- Masuoka J, Brandner S, Paulus W, Soffer D, Vital A, Chimelli L, Jouvet A, Yonekawa Y, Kleihues P, Ohgaki H: Germline SDHD mutation in paraganglioma of the spinal cord. Oncogene. 2001 Aug 16;20(36):5084-6. [PubMed
]
- Kytola S, Nord B, Elder EE, Carling T, Kjellman M, Cedermark B, Juhlin C, Hoog A, Isola J, Larsson C: Alterations of the SDHD gene locus in midgut carcinoids, Merkel cell carcinomas, pheochromocytomas, and abdominal paragangliomas. Genes Chromosomes Cancer. 2002 Jul;34(3):325-32. [PubMed
]
- Gimenez-Roqueplo AP, Favier J, Rustin P, Rieubland C, Crespin M, Nau V, Khau Van Kien P, Corvol P, Plouin PF, Jeunemaitre X: Mutations in the SDHB gene are associated with extra-adrenal and/or malignant phaeochromocytomas. Cancer Res. 2003 Sep 1;63(17):5615-21. [PubMed
]
- Neumann HP, Bausch B, McWhinney SR, Bender BU, Gimm O, Franke G, Schipper J, Klisch J, Altehoefer C, Zerres K, Januszewicz A, Eng C, Smith WM, Munk R, Manz T, Glaesker S, Apel TW, Treier M, Reineke M, Walz MK, Hoang-Vu C, Brauckhoff M, Klein-Franke A, Klose P, Schmidt H, Maier-Woelfle M, Peczkowska M, Szmigielski C, Eng C: Germ-line mutations in nonsyndromic pheochromocytoma. N Engl J Med. 2002 May 9;346(19):1459-66. [PubMed
]
- Cascon A, Ruiz-Llorente S, Cebrian A, Leton R, Telleria D, Benitez J, Robledo M: G12S and H50R variations are polymorphisms in the SDHD gene. Genes Chromosomes Cancer. 2003 Jun;37(2):220-1. [PubMed
]
- Neumann HP, Pawlu C, Peczkowska M, Bausch B, McWhinney SR, Muresan M, Buchta M, Franke G, Klisch J, Bley TA, Hoegerle S, Boedeker CC, Opocher G, Schipper J, Januszewicz A, Eng C: Distinct clinical features of paraganglioma syndromes associated with SDHB and SDHD gene mutations. JAMA. 2004 Aug 25;292(8):943-51. [PubMed
]
- Leube B, Huber R, Goecke TO, Sandmann W, Royer-Pokora B: SDHD mutation analysis in seven German patients with sporadic carotid body paraganglioma: one novel mutation, no Dutch founder mutation and further evidence that G12S is a polymorphism. Clin Genet. 2004 Jan;65(1):61-3. [PubMed
]
- McWhinney SR, Pasini B, Stratakis CA: Familial gastrointestinal stromal tumors and germ-line mutations. N Engl J Med. 2007 Sep 6;357(10):1054-6. [PubMed
]
- Ni Y, Zbuk KM, Sadler T, Patocs A, Lobo G, Edelman E, Platzer P, Orloff MS, Waite KA, Eng C: Germline mutations and variants in the succinate dehydrogenase genes in Cowden and Cowden-like syndromes. Am J Hum Genet. 2008 Aug;83(2):261-8. [PubMed
]
- Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5425 |
| Enzyme 4 Name |
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial |
| Enzyme 4 Synonyms |
- Iron-sulfur subunit of complex II
- Ip
|
| Enzyme 4 Gene Name |
SDHB |
| Enzyme 4 Protein Sequence |
>Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
MAAVVALSLRRRLPATTLGGACLQASRGAQTAAATAPRIKKFAIYRWDPDKAGDKPHMQT
YEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN
LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKL
DGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSL
YRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKASV
|
| Enzyme 4 Number of Residues |
280 |
| Enzyme 4 Molecular Weight |
31629.4 |
| Enzyme 4 Theoretical pI |
8.92 |
| Enzyme 4 GO Classification |
| Function |
- binding
- catalytic activity
- electron carrier activity
- iron-sulfur cluster binding
- metal cluster binding
- oxidoreductase activity
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- oxidation reduction
- tricarboxylic acid cycle
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in electron carrier activity |
| Enzyme 4 Specific Function |
Iron-sulfur protein (IP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- succinate + ubiquinone = fumarate + ubiquinol [RN:R02164]
|
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
189065269  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P21912  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
DHSB_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>843 bp
ATGGCGGCGGTGGTCGCACTCTCCTTGAGGCGCCGGTTGCCGGCCACAACCCTTGGCGGA
GCCTGCCTGCAGGCCTCCCGAGGAGCCCAGACAGCTGCAGCCACAGCTCCCCGTATCAAG
AAATTTGCCATCTATCGATGGGACCCAGACAAGGCTGGAGACAAACCTCATATGCAGACT
TATGAAGTTGACCTTAATAAATGTGGCCCCATGGTATTGGATGCTTTAATCAAGATTAAG
AATGAAGTTGACTCTACTTTGACCTTCCGAAGATCATGCAGAGAAGGCATCTGTGGCTCT
TGTGCAATGAACATCAATGGAGGCAACACTCTAGCTTGCACCCGAAGGATTGACACCAAC
CTCAATAAGGTCTCAAAAATCTACCCTCTTCCACACATGTATGTGATAAAGGATCTTGTT
CCCGATTTGAGCAACTTCTATGCACAGTACAAATCCATTGAGCCTTATTTGAAGAAGAAG
GATGAATCTCAGGAAGGCAAGCAGCAGTATCTGCAGTCCATAGAAGAGCGTGAGAAACTG
GACGGGCTCTACGAGTGCATTCTCTGTGCCTGCTGTAGCACCAGCTGCCCCAGCTACTGG
TGGAACGGAGACAAATATCTGGGGCCTGCAGTTCTTATGCAGGCCTATCGCTGGATGATT
GACTCCAGAGATGACTTCACAGAGGAGCGCCTGGCCAAGCTGCAGGACCCATTCTCTCTA
TACCGCTGCCACACCATCATGAACTGCACAAGGACCTGTCCTAAGGGTCTGAATCCAGGG
AAAGCTATTGCAGAGATCAAGAAAATGATGGCAACCTATAAGGAGAAGAAAGCTTCAGTT
TAA
|
| Enzyme 4 GenBank Gene ID |
AK312056  |
| Enzyme 4 GeneCard ID |
SDHB  |
| Enzyme 4 GenAtlas ID |
SDHB  |
| Enzyme 4 HGNC ID |
HGNC:10681  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p36.1-p35 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Au HC, Ream-Robinson D, Bellew LA, Broomfield PL, Saghbini M, Scheffler IE: Structural organization of the gene encoding the human iron-sulfur subunit of succinate dehydrogenase. Gene. 1995 Jul 4;159(2):249-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kita K, Oya H, Gennis RB, Ackrell BA, Kasahara M: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of iron sulfur (Ip) subunit of liver mitochondria. Biochem Biophys Res Commun. 1990 Jan 15;166(1):101-8. [PubMed
]
- Gould SJ, Subramani S, Scheffler IE: Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1934-8. [PubMed
]
- Astuti D, Latif F, Dallol A, Dahia PL, Douglas F, George E, Skoldberg F, Husebye ES, Eng C, Maher ER: Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma. Am J Hum Genet. 2001 Jul;69(1):49-54. Epub 2001 Jun 12. [PubMed
]
- Young AL, Baysal BE, Deb A, Young WF Jr: Familial malignant catecholamine-secreting paraganglioma with prolonged survival associated with mutation in the succinate dehydrogenase B gene. J Clin Endocrinol Metab. 2002 Sep;87(9):4101-5. [PubMed
]
- Baysal BE, Willett-Brozick JE, Lawrence EC, Drovdlic CM, Savul SA, McLeod DR, Yee HA, Brackmann DE, Slattery WH 3rd, Myers EN, Ferrell RE, Rubinstein WS: Prevalence of SDHB, SDHC, and SDHD germline mutations in clinic patients with head and neck paragangliomas. J Med Genet. 2002 Mar;39(3):178-83. [PubMed
]
- Neumann HP, Bausch B, McWhinney SR, Bender BU, Gimm O, Franke G, Schipper J, Klisch J, Altehoefer C, Zerres K, Januszewicz A, Eng C, Smith WM, Munk R, Manz T, Glaesker S, Apel TW, Treier M, Reineke M, Walz MK, Hoang-Vu C, Brauckhoff M, Klein-Franke A, Klose P, Schmidt H, Maier-Woelfle M, Peczkowska M, Szmigielski C, Eng C: Germ-line mutations in nonsyndromic pheochromocytoma. N Engl J Med. 2002 May 9;346(19):1459-66. [PubMed
]
- Gimenez-Roqueplo AP, Favier J, Rustin P, Rieubland C, Crespin M, Nau V, Khau Van Kien P, Corvol P, Plouin PF, Jeunemaitre X: Mutations in the SDHB gene are associated with extra-adrenal and/or malignant phaeochromocytomas. Cancer Res. 2003 Sep 1;63(17):5615-21. [PubMed
]
- Astuti D, Hart-Holden N, Latif F, Lalloo F, Black GC, Lim C, Moran A, Grossman AB, Hodgson SV, Freemont A, Ramsden R, Eng C, Evans DG, Maher ER: Genetic analysis of mitochondrial complex II subunits SDHD, SDHB and SDHC in paraganglioma and phaeochromocytoma susceptibility. Clin Endocrinol (Oxf). 2003 Dec;59(6):728-33. [PubMed
]
- Benn DE, Croxson MS, Tucker K, Bambach CP, Richardson AL, Delbridge L, Pullan PT, Hammond J, Marsh DJ, Robinson BG: Novel succinate dehydrogenase subunit B (SDHB) mutations in familial phaeochromocytomas and paragangliomas, but an absence of somatic SDHB mutations in sporadic phaeochromocytomas. Oncogene. 2003 Mar 6;22(9):1358-64. [PubMed
]
- McDonnell CM, Benn DE, Marsh DJ, Robinson BG, Zacharin MR: K40E: a novel succinate dehydrogenase (SDH)B mutation causing familial phaeochromocytoma and paraganglioma. Clin Endocrinol (Oxf). 2004 Oct;61(4):510-4. [PubMed
]
- Neumann HP, Pawlu C, Peczkowska M, Bausch B, McWhinney SR, Muresan M, Buchta M, Franke G, Klisch J, Bley TA, Hoegerle S, Boedeker CC, Opocher G, Schipper J, Januszewicz A, Eng C: Distinct clinical features of paraganglioma syndromes associated with SDHB and SDHD gene mutations. JAMA. 2004 Aug 25;292(8):943-51. [PubMed
]
- Maier-Woelfle M, Brandle M, Komminoth P, Saremaslani P, Schmid S, Locher T, Heitz PU, Krull I, Galeazzi RL, Schmid C, Perren A: A novel succinate dehydrogenase subunit B gene mutation, H132P, causes familial malignant sympathetic extraadrenal paragangliomas. J Clin Endocrinol Metab. 2004 Jan;89(1):362-7. [PubMed
]
- van Nederveen FH, Korpershoek E, Lenders JW, de Krijger RR, Dinjens WN: Somatic SDHB mutation in an extraadrenal pheochromocytoma. N Engl J Med. 2007 Jul 19;357(3):306-8. [PubMed
]
- McWhinney SR, Pasini B, Stratakis CA: Familial gastrointestinal stromal tumors and germ-line mutations. N Engl J Med. 2007 Sep 6;357(10):1054-6. [PubMed
]
- Ni Y, Zbuk KM, Sadler T, Patocs A, Lobo G, Edelman E, Platzer P, Orloff MS, Waite KA, Eng C: Germline mutations and variants in the succinate dehydrogenase genes in Cowden and Cowden-like syndromes. Am J Hum Genet. 2008 Aug;83(2):261-8. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5481 |
| Enzyme 5 Name |
Succinate-semialdehyde dehydrogenase, mitochondrial |
| Enzyme 5 Synonyms |
- Aldehyde dehydrogenase family 5 member A1
- NAD(+)-dependent succinic semialdehyde dehydrogenase
|
| Enzyme 5 Gene Name |
ALDH5A1 |
| Enzyme 5 Protein Sequence |
>Succinate-semialdehyde dehydrogenase, mitochondrial
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLR
TDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER
SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIH
TPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL
AELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV
KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF
AEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFF
EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR
VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
|
| Enzyme 5 Number of Residues |
535 |
| Enzyme 5 Molecular Weight |
57214.2 |
| Enzyme 5 Theoretical pI |
8.37 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in oxidoreductase activity |
| Enzyme 5 Specific Function |
Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+ [RN:R00713]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
3766467  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P51649  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
SSDH_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1608 bp
ATGGCGACCTGCATTTGGCTGCGGAGCTGTGGGGCCCGGCGCCTCGGGTCGACGTTTCCA
GGCTGCCGCCTCCGCCCCCGCGCCGGCGGCCTGGTCCCTGCCTCCGGGCCTGCGCCCGGC
CCGGCCCAGCTCCGCTGCTACGCTGGGCGCCTGGCGGGCCTCTCTGCGGCGCTGCTGCGC
ACCGACAGCTTCGTGGGCGGCCGCTGGCTCCCGGCCGCCGCCACCTTCCCCGTGCAAGAC
CCGGCCAGCGGCGCCGCTCTGGGCATGGTAGCCGACTGCGGGGTGCGAGAGGCCCGCGCC
GCCGTGCGCGCTGCCTACGAGGCTTTCTGCCGCTGGAGGGAGGTCTCCGCCAAGGAGAGG
AGTTCATTACTTCGGAAGTGGTACAATTTAATGATACAAAATAAGGATGACCTTGCCAGA
ATAATCACAGCTGAAAGTGGAAAGCCACTGAAGGAGGCACATGGAGAAATTCTCTATTCC
GCCTTTTTCCTAGAGTGGTTCTCTGAGGAAGCCCGCCGTGTTTACGGAGACATTATCCAC
ACCCCGGCAAAGGACAGGCGGGCCCTGGTCCTCAAGCAGCCCATAGGCGTGGCTGCAGTC
ATCACCCCGTGGAATTTCCCCAGTGCCATGATCACCCGGAAGGTGGGGGCCGCCCTGGCA
GCCGGCTGTACTGTCGTGGTGAAGCCTGCCGAAGACACGCCCTTCTCCGCCCTGGCCCTG
GCTGAGCTTGCAAGCCAGGCTGGGATTCCTTCAGGTGTATACAATGTTATTCCCTGTTCT
CGAAAGAATGCCAAGGAAGTAGGGGAGGCAATTTGTACTGATCCTCTGGTGTCCAAAATT
TCCTTTACTGGTTCAACAACTACAGGAAAGATCCTGTTGCACCACGCAGCAAACTCTGTG
AAAAGGGTCTCTATGGAGCTGGGCGGCCTTGCTCCATTTATAGTATTTGACAGTGCCAAC
GTGGACCAGGCTGTAGCAGGGGCCATGGCATCTAAATTTAGGAACACTGGACAGACTTGT
GTTTGCTCAAACCAATTCTTGGTGCAAAGGGGCATCCATGATGCCTTTGTAAAAGCATTC
GCCGAGGCCATGAAGAAGAACCTGCGCGTAGGTAATGGATTTGAGGAAGGAACTACTCAG
GGCCCATTAATTAATGAAAAAGCGGTAGAAAAGGTGGAGAAACAGGTGAATGATGCCGTT
TCTAAAGGTGCCACCGTTGTGACAGGTGGAAAACGACACCAACTTGGAAAAAATTTCTTT
GAGCCTACCCTGCTGTGCAATGTCACCCAGGACATGCTGTGCACTCATGAAGAGACTTTC
GGGCCTCTGGCACCAGTTATCAAGTTCGATACAGAGGAGGAGGCTATAGCAATCGCTAAC
GCAGCTGATGTTGGGTTAGCAGGTTATTTTTACTCTCAAGACCCAGCCCAGATCTGGAGA
GTGGCAGAGCAGCTGGAAGTGGGCATGGTTGGCGTCAACGAAGGATTAATTTCCTCTGTG
GAGTGCCCTTTTGGTGGAGTGAAGCAGTCCGGCCTTGGGCGAGAGGGGTCCAAGTATGGC
ATTGATGAGTATCTGGAACTCAAGTATGTGTGTTACGGGGGCTTGTAG
|
| Enzyme 5 GenBank Gene ID |
Y11192  |
| Enzyme 5 GeneCard ID |
ALDH5A1  |
| Enzyme 5 GenAtlas ID |
ALDH5A1  |
| Enzyme 5 HGNC ID |
HGNC:408  |
| Enzyme 5 Chromosome Location |
6 |
| Enzyme 5 Locus |
6p22.2-p22.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Chambliss KL, Hinson DD, Trettel F, Malaspina P, Novelletto A, Jakobs C, Gibson KM: Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria). Am J Hum Genet. 1998 Aug;63(2):399-408. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chambliss KL, Caudle DL, Hinson DD, Moomaw CR, Slaughter CA, Jakobs C, Gibson KM: Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J Biol Chem. 1995 Jan 6;270(1):461-7. [PubMed
]
- Trettel F, Malaspina P, Jodice C, Novelletto A, Slaughter CA, Caudle DL, Hinson DD, Chambliss KL, Gibson KM: Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization. Adv Exp Med Biol. 1997;414:253-60. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Kim YG, Lee S, Kwon OS, Park SY, Lee SJ, Park BJ, Kim KJ: Redox-switch modulation of human SSADH by dynamic catalytic loop. EMBO J. 2009 Apr 8;28(7):959-68. Epub 2009 Mar 19. [PubMed
]
- Hogema BM, Akaboshi S, Taylor M, Salomons GS, Jakobs C, Schutgens RB, Wilcken B, Worthington S, Maropoulos G, Grompe M, Gibson KM: Prenatal diagnosis of succinic semialdehyde dehydrogenase deficiency: increased accuracy employing DNA, enzyme, and metabolite analyses. Mol Genet Metab. 2001 Mar;72(3):218-22. [PubMed
]
- Aoshima T, Kajita M, Sekido Y, Ishiguro Y, Tsuge I, Kimura M, Yamaguchi S, Watanabe K, Shimokata K, Niwa T: Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency: a compound heterozygote with 103-121del and 1460T > A of the ALDH5A1 gene. Hum Hered. 2002;53(1):42-4. [PubMed
]
- Akaboshi S, Hogema BM, Novelletto A, Malaspina P, Salomons GS, Maropoulos GD, Jakobs C, Grompe M, Gibson KM: Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency. Hum Mutat. 2003 Dec;22(6):442-50. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5537 |
| Enzyme 6 Name |
Prolyl 4-hydroxylase subunit alpha-2 |
| Enzyme 6 Synonyms |
- 4-PH alpha-2
- Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2
|
| Enzyme 6 Gene Name |
P4HA2 |
| Enzyme 6 Protein Sequence |
>Prolyl 4-hydroxylase subunit alpha-2
MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKS
WANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQR
QFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEG
DYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSH
ERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVK
LTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPK
LARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVAN
YGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKK
GTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD
|
| Enzyme 6 Number of Residues |
535 |
| Enzyme 6 Molecular Weight |
60901.4 |
| Enzyme 6 Theoretical pI |
5.43 |
| Enzyme 6 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
- peptidyl-proline dioxygenase activity
- procollagen-proline 4-dioxygenase activity
- procollagen-proline dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 6 General Function |
Involved in oxidoreductase activity |
| Enzyme 6 Specific Function |
Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins |
| Enzyme 6 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 6 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O15460  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
P4HA2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1608 bp
ATGAAACTCTGGGTGTCTGCATTGCTGATGGCCTGGTTTGGTGTCCTGAGCTGTGTGCAG
GCCGAATTCTTCACCTCTATTGGGCACATGACTGACCTGATTTATGCAGAGAAAGAGCTG
GTGCAGTCTCTGAAAGAGTACATCCTTGTGGAGGAAGCCAAGCTTTCCAAGATTAAGAGC
TGGGCCAACAAAATGGAAGCCTTGACTAGCAAGTCAGCTGCTGATGCTGAGGGCTACCTG
GCTCACCCTGTGAATGCCTACAAACTGGTGAAGCGGCTAAACACAGACTGGCCTGCGCTG
GAGGACCTTGTCCTGCAGGACTCAGCTGCAGGTTTTATCGCCAACCTCTCTGTGCAGCGG
CAGTTCTTCCCCACTGATGAGGACGAGATAGGAGCTGCCAAAGCCCTGATGAGACTTCAG
GACACATACAGGCTGGACCCAGGCACAATTTCCAGAGGGGAACTTCCAGGAACCAAGTAC
CAGGCAATGCTGAGTGTGGATGACTGCTTTGGGATGGGCCGCTCGGCCTACAATGAAGGG
GACTATTATCATACGGTGTTGTGGATGGAGCAGGTGCTAAAGCAGCTTGATGCCGGGGAG
GAGGCCACCACAACCAAGTCACAGGTGCTGGACTACCTCAGCTATGCTGTCTTCCAGTTG
GGTGATCTGCACCGTGCCCTGGAGCTCACCCGCCGCCTGCTCTCCCTTGACCCAAGCCAC
GAACGAGCTGGAGGGAATCTGCGGTACTTTGAGCAGTTATTGGAGGAAGAGAGAGAAAAA
ACGTTAACAAATCAGACAGAAGCTGAGCTAGCAACCCCAGAAGGCATCTATGAGAGGCCT
GTGGACTACCTGCCTGAGAGGGATGTTTACGAGAGCCTCTGTCGTGGGGAGGGTGTCAAA
CTGACACCCCGTAGACAGAAGAGGCTTTTCTGTAGGTACCACCATGGCAACAGGGCCCCA
CAGCTGCTCATTGCCCCCTTCAAAGAGGAGGACGAGTGGGACAGCCCGCACATCGTCAGG
TACTACGATGTCATGTCTGATGAGGAAATCGAGAGGATCAAGGAGATCGCAAAACCTAAA
CTTGCACGAGCCACCGTTCGTGATCCCAAGACAGGAGTCCTCACTGTCGCCAGCTACCGG
GTTTCCAAAAGCTCCTGGCTAGAGGAAGATGATGACCCTGTTGTGGCCCGAGTAAATCGT
CGGATGCAGCATATCACAGGGTTAACAGTAAAGACTGCAGAATTGTTACAGGTTGCAAAT
TATGGAGTGGGAGGACAGTATGAACCGCACTTCGACTTCTCTAGGAATGATGAGCGAGAT
ACTTTCAAGCATTTAGGGACGGGGAATCGTGTGGCTACTTTCTTAAACTACATGAGTGAT
GTAGAAGCTGGTGGTGCCACCGTCTTCCCTGATCTGGGGGCTGCAATTTGGCCTAAGAAG
GGTACAGCTGTGTTCTGGTACAACCTCTTGCGGAGCGGGGAAGGTGACTACCGAACAAGA
CATGCTGCCTGCCCTGTGCTTGTGGGCTGCAAGTGGGTCTCCAATAAGTGGTTCCATGAA
CGAGGACAGGAGTTCTTGAGACCTTGTGGATCAACAGAAGTTGACTGA
|
| Enzyme 6 GenBank Gene ID |
U90441  |
| Enzyme 6 GeneCard ID |
P4HA2  |
| Enzyme 6 GenAtlas ID |
P4HA2  |
| Enzyme 6 HGNC ID |
HGNC:8547  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q31 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997 Jul 11;272(28):17342-8. [PubMed
]
- Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J: Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues. Eur J Biochem. 2001 Oct;268(20):5300-9. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5539 |
| Enzyme 7 Name |
Prolyl 4-hydroxylase subunit alpha-1 |
| Enzyme 7 Synonyms |
- 4-PH alpha-1
- Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1
|
| Enzyme 7 Gene Name |
P4HA1 |
| Enzyme 7 Protein Sequence |
>Prolyl 4-hydroxylase subunit alpha-1
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWA
EKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQY
FPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADY
YHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQR
ANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKM
TPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRL
RRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANY
GVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKG
TAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
|
| Enzyme 7 Number of Residues |
534 |
| Enzyme 7 Molecular Weight |
61048.8 |
| Enzyme 7 Theoretical pI |
5.84 |
| Enzyme 7 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
- peptidyl-proline dioxygenase activity
- procollagen-proline 4-dioxygenase activity
- procollagen-proline dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 7 General Function |
Involved in oxidoreductase activity |
| Enzyme 7 Specific Function |
Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins |
| Enzyme 7 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 7 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
55666281  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P13674  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
P4HA1_HUMAN  |
| Enzyme 7 PDB ID |
1TJC  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1605 bp
ATGATCTGGTATATATTAATTATAGGAATTCTGCTTCCCCAGTCTTTGGCTCATCCAGGC
TTTTTTACTTCAATTGGTCAGATGACTGATTTGATCCATACTGAGAAAGATCTGGTGACT
TCTCTGAAAGATTATATTAAGGCAGAAGAGGACAAGTTAGAACAAATAAAAAAATGGGCA
GAGAAGTTAGATCGGCTAACTAGTACAGCGACAAAAGATCCAGAAGGATTTGTTGGGCAT
CCAGTAAATGCATTCAAATTAATGAAACGTCTGAATACTGAGTGGAGTGAGTTGGAGAAT
CTGGTCCTTAAGGATATGTCAGATGGCTTTATCTCTAACCTAACCATTCAGAGACAGTAC
TTTCCTAATGATGAAGATCAGGTTGGGGCAGCCAAAGCTCTGTTACGTCTCCAGGATACC
TACAATTTGGATACAGATACCATCTCAAAGGGTAATCTTCCAGGAGTGAAACACAAATCT
TTTCTAACGGCTGAGGACTGCTTTGAGTTGGGCAAAGTGGCCTATACAGAAGCAGATTAT
TACCATACGGAACTGTGGATGGAACAAGCCCTAAGGCAACTGGATGAAGGCGAGATTTCT
ACCATAGATAAAGTCTCTGTTCTAGATTATTTGAGCTATGCGGTATATCAGCAGGGAGAC
CTGGATAAGGCACTTTTGCTCACAAAGAAGCTTCTTGAACTAGATCCTGAACATCAGAGA
GCTAATGGTAACTTAAAATATTTTGAGTATATAATGGCTAAAGAAAAAGATGTCAATAAG
TCTGCTTCAGATGACCAATCTGATCAGAAAACTACACCAAAGAAAAAAGGGGTTGCTGTG
GATTACCTGCCAGAGAGACAGAAGTACGAAATGCTGTGCCGTGGGGAGGGTATCAAAATG
ACCCCTCGGAGACAGAAAAAACTCTTTTGCCGCTACCATGATGGAAACCGTAATCCTAAA
TTTATTCTGGCTCCAGCTAAACAGGAGGATGAATGGGACAAGCCTCGTATTATTCGCTTC
CATGATATTATTTCTGATGCAGAAATTGAAATCGTCAAAGACCTAGCAAAACCAAGGCTG
AGCCGAGCTACAGTACATGACCCTGAGACTGGAAAATTGACCACAGCACAGTACAGAGTA
TCTAAGAGTGCCTGGCTCTCTGGCTATGAAAATCCTGTGGTGTCTCGAATTAATATGAGA
ATACAAGATCTAACAGGACTAGATGTTTCCACAGCAGAGGAATTACAGGTAGCAAATTAT
GGAGTTGGAGGACAGTATGAACCCCATTTTGACTTTGCACGGAAAGATGAGCCAGATGCT
TTCAAAGAGCTGGGGACAGGAAATAGAATTGCTACATGGCTGTTTTATATGAGTGATGTG
TCTGCAGGAGGAGCCACTGTTTTTCCTGAAGTTGGAGCTAGTGTTTGGCCCAAAAAAGGA
ACTGCTGTTTTCTGGTATAATCTGTTTGCCAGTGGAGAAGGAGATTATAGTACACGGCAT
GCAGCCTGTCCAGTGCTAGTTGGCAACAAATGGGTATCCAATAAATGGCTCCATGAACGT
GGACAAGAATTTCGAAGACCTTGTACGTTGTCAGAATTGGAATGA
|
| Enzyme 7 GenBank Gene ID |
AL731563  |
| Enzyme 7 GeneCard ID |
P4HA1  |
| Enzyme 7 GenAtlas ID |
P4HA1  |
| Enzyme 7 HGNC ID |
HGNC:8546  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
10q21.3-q23.1 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Helaakoski T, Vuori K, Myllyla R, Kivirikko KI, Pihlajaniemi T: Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4392-6. [PubMed
]
- Helaakoski T, Veijola J, Vuori K, Rehn M, Chow LT, Taillon-Miller P, Kivirikko KI, Pihlajaniemi T: Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues. J Biol Chem. 1994 Nov 11;269(45):27847-54. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J: The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues. J Biol Chem. 2004 Dec 10;279(50):52255-61. Epub 2004 Sep 28. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5619 |
| Enzyme 8 Name |
Gamma-butyrobetaine dioxygenase |
| Enzyme 8 Synonyms |
- Gamma-butyrobetaine hydroxylase
- Gamma-BBH
- Gamma-butyrobetaine,2-oxoglutarate dioxygenase
|
| Enzyme 8 Gene Name |
BBOX1 |
| Enzyme 8 Protein Sequence |
>Gamma-butyrobetaine dioxygenase
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
|
| Enzyme 8 Number of Residues |
387 |
| Enzyme 8 Molecular Weight |
44714.6 |
| Enzyme 8 Theoretical pI |
6.73 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- transition metal ion binding
|
| Process |
- betaine metabolic process
- carnitine biosynthetic process
- carnitine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in iron ion binding |
| Enzyme 8 Specific Function |
Catalyzes the formation of L-carnitine from gamma- butyrobetaine |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2 [RN:R02397]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O75936  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
BODG_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1164 bp
ATGGCTTGTACCATCCAAAAGGCAGAAGCACTTGACGGGGCTCATTTGATGCAGATCCTC
TGGTATGATGAGGAAGAGTCTCTCTACCCAGCTGTATGGTTGAGAGACAACTGTCCGTGC
TCTGATTGCTACCTGGATTCTGCAAAAGCACGGAAACTTCTAGTGGAAGCTCTTGATGTG
AACATTGGAATTAAAGGCTTGATATTTGACAGAAAAAAGGTGTACATCACATGGCCCGAT
GAGCATTACAGTGAATTCCAGGCTGATTGGCTGAAGAAAAGATGCTTTTCCAAGCAGGCC
AGAGCAAAGCTCCAAAGAGAATTGTTTTTTCCAGAATGCCAATACTGGGGCTCAGAGCTC
CAGCTACCCACTTTGGATTTTGAAGATGTTTTAAGATATGATGAACATGCATACAAGTGG
CTCTCCACCCTCAAGAAAGTAGGCATAGTAAGACTCACCGGAGCATCTGACAAACCAGGA
GAAGTTTCAAAACTTGGGAAAAGGATGGGTTTCCTCTATCTCACATTTTATGGACATACT
TGGCAAGTGCAAGACAAAATCGATGCAAACAATGTGGCTTACACAACTGGGAAGCTAAGC
TTTCACACTGATTATCCAGCCCTCCATCATCCACCTGGGGTTCAGCTTCTTCACTGCATA
AAGCAAACAGTCACAGGGGGTGATTCAGAAATTGTAGATGGGTTTAATGTGTGCCAAAAA
CTAAAGAAAAATAATCCTCAGGCATTCCAGATTTTGTCCTCTACCTTTGTGGACTTTACA
GACATTGGAGTGGATTACTGTGATTTTTCTGTACAATCAAAACATAAAATTATAGAGTTA
GATGATAAAGGCCAAGTGGTTCGCATCAACTTCAATAACGCAACTAGGGACACAATATTT
GATGTACCTGTTGAAAGAGTTCAGCCTTTTTATGCTGCTCTGAAGGAGTTTGTTGACCTC
ATGAACAGCAAAGAATCCAAGTTTACCTTCAAGATGAATCCAGGTGATGTGATTACTTTT
GATAACTGGCGCTTACTTCATGGCCGACGTAGCTATGAAGCAGGAACTGAGATATCCCGC
CATCTAGAAGGAGCTTATGCTGACTGGGATGTGGTCATGTCAAGGCTTCGTATCTTAAGG
CAGAGGGTGGAGAATGGAAACTGA
|
| Enzyme 8 GenBank Gene ID |
AF082868  |
| Enzyme 8 GeneCard ID |
BBOX1  |
| Enzyme 8 GenAtlas ID |
BBOX1  |
| Enzyme 8 HGNC ID |
HGNC:964  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
11p14.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Vaz FM, van Gool S, Ofman R, Ijlst L, Wanders RJ: Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase. Biochem Biophys Res Commun. 1998 Sep 18;250(2):506-10. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5699 |
| Enzyme 9 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 |
| Enzyme 9 Synonyms |
- Lysyl hydroxylase 1
- LH1
|
| Enzyme 9 Gene Name |
PLOD1 |
| Enzyme 9 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGL
GEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQA
RSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQ
LFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLI
HGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPF
VSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANAD
ARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWG
ALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPD
MAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYT
KALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTID
IHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDAS
TFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYI
AVSFVDP
|
| Enzyme 9 Number of Residues |
727 |
| Enzyme 9 Molecular Weight |
83549.5 |
| Enzyme 9 Theoretical pI |
6.94 |
| Enzyme 9 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 9 General Function |
Involved in oxidoreductase activity |
| Enzyme 9 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
20149013  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q02809  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PLOD1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>2184 bp
ATGCGGCCCCTGCTGCTACTGGCCCTGCTGGGCTGGCTGCTGCTGGCCGAAGCGAAGGGC
GACGCCAAGCCGGAGGACAACCTTTTAGTCCTCACGGTGGCCACTAAGGAGACCGAGGGA
TTCCGTCGCTTCAAGCGCTCAGCTCAGTTCTTCAACTACAAGATCCAGGCGCTTGGCCTA
GGGGAGGACTGGAATGTGGAGAAGGGGACGTCGGCAGGTGGAGGGCAGAAGGTCCGGCTG
CTGAAGAAAGCTCTGGAGAAGCACGCAGACAAGGAGGATCTGGTCATTCTCTTTGCAGAC
AGCTATGACGTGCTGTTTGCATCGGGGCCCCGGGAGCTCCTGAAGAAGTTCCGGCAGGCC
AGGAGCCAGGTGGTCTTCTCTGCTGAGGAGCTCATCTACCCAGACCGCAGGCTGGAGACC
AAGTATCCGGTGGTGTCCGATGGCAAGAGGTTCCTGGGCTCTGGAGGCTTCATCGGTTAT
GCCCCCAACCTCAGCAAACTGGTGGCCGAGTGGGAGGGCCAGGACAGCGACAGCGATCAG
CTGTTTTACACCAAGATCTTCTTGGACCCGGAGAAGAGGGAGCAGATCAATATCACCCTG
GACCACCGCTGCCGTATCTTCCAGAACCTGGATGGAGCCTTGGATGAGGTCGTGCTCAAG
TTTGAAATGGGCCATGTGAGAGCGAGGAACCTGGCCTATGACACCCTCCCGGTCCTGATC
CATGGCAACGGGCCAACCAAGCTGCAGTTGAACTACCTGGGCAACTACATCCCGCGCTTC
TGGACCTTCGAAACAGGCTGCACCGTGTGTGACGAAGGCTTGCGCAGCCTCAAGGGCATT
GGGGATGAAGCTCTGCCCACGGTCCTGGTCGGCGTGTTCATCGAACAGCCCACGCCGTTT
GTGTCCCTGTTCTTCCAGCGGCTCCTGCGGCTCCACTACCCCCAGAAACACATGCGACTT
TTCATCCACAACCACGAGCAGCACCACAAGGCTCAGGTGGAAGAGTTCCTGGCACAGCAT
GGCAGCGAGTACCAGTCTGTGAAGCTGGTGGGCCCTGAGGTGCGGATGGCGAATGCAGAT
GCCAGGAACATGGGCGCAGACCTGTGCCGGCAGGACCGCAGCTGCACCTACTACTTCAGC
GTGGATGCTGACGTGGCCCTGACCGAGCCCAACAGCCTGCGGCTGCTGATCCAACAGAAC
AAGAATGTCATTGCCCCGCTGATGACCCGGCATGGGAGGCTGTGGTCGAACTTCTGGGGG
GCTCTCAGTGCAGATGGCTACTATGCCCGTTCCGAGGACTACGTGGACATTGTGCAGGGG
CGGCGTGTTGGTGTCTGGAATGTGCCCTATATTTCAAACATCTACTTGATCAAGGGCAGT
GCCCTGCGGGGTGAGCTGCAGTCCTCAGATCTCTTCCACCACAGCAAGCTGGACCCCGAC
ATGGCCTTCTGTGCCAACATCCGGCAGCAGGATGTGTTCATGTTCCTGACCAACCGGCAC
ACCCTTGGCCATCTGCTCTCCCTAGACAGCTACCGCACCACCCACCTGCACAACGACCTC
TGGGAGGTGTTCAGCAACCCCGAGGACTGGAAGGAGAAGTACATCCACCAGAACTACACC
AAAGCCCTGGCAGGGAAGCTGGTGGAGACGCCCTGCCCGGATGTCTATTGGTTCCCCATC
TTCACGGAGGTGGCCTGTGATGAGCTGGTGGAGGAGATGGAGCACTTTGGCCAGTGGTCT
CTGGGCAACAACAAGGACAACCGCATCCAGGGTGGCTACGAGAACGTGCCGACTATTGAC
ATCCACATGAACCAGATCGGCTTTGAGCGGGAGTGGCACAAATTCCTGCTGGAGTACATT
GCGCCCATGACGGAGAAGCTCTACCCCGGCTACTACACCAGGGCCCAGTTTGACCTGGCC
TTTGTCGTCCGCTACAAGCCTGATGAGCAGCCCTCACTGATGCCACACCATGATGCCTCC
ACCTTCACCATCAACATCGCCCTGAACCGAGTCGGGGTGGATTACGAGGGCGGGGGCTGT
CGGTTCCTGCGCTACAACTGTTCCATCCGAGCCCCAAGGAAGGGCTGGACCCTCATGCAC
CCTGGACGACTCACGCATTACCATGAGGGGCTCCCCACCACCAGGGGCACCCGCTACATC
GCAGTCTCCTTCGTCGATCCCTAA
|
| Enzyme 9 GenBank Gene ID |
AF490527  |
| Enzyme 9 GeneCard ID |
PLOD1  |
| Enzyme 9 GenAtlas ID |
PLOD1  |
| Enzyme 9 HGNC ID |
HGNC:9081  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.22 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Hautala T, Byers MG, Eddy RL, Shows TB, Kivirikko KI, Myllyla R: Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2. Genomics. 1992 May;13(1):62-9. [PubMed
]
- Heikkinen J, Hautala T, Kivirikko KI, Myllyla R: Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients. Genomics. 1994 Dec;24(3):464-71. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Pirskanen A, Kaimio AM, Myllyla R, Kivirikko KI: Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. J Biol Chem. 1996 Apr 19;271(16):9398-402. [PubMed
]
- Ha VT, Marshall MK, Elsas LJ, Pinnell SR, Yeowell HN: A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene. J Clin Invest. 1994 Apr;93(4):1716-21. [PubMed
]
- Brinckmann J, Acil Y, Feshchenko S, Katzer E, Brenner R, Kulozik A, Kugler S: Ehlers-Danlos syndrome type VI: lysyl hydroxylase deficiency due to a novel point mutation (W612C). Arch Dermatol Res. 1998 Apr;290(4):181-6. [PubMed
]
- Yeowell HN, Allen JD, Walker LC, Overstreet MA, Murad S, Thai SF: Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Matrix Biol. 2000 Feb;19(1):37-46. [PubMed
]
- Giunta C, Randolph A, Al-Gazali LI, Brunner HG, Kraenzlin ME, Steinmann B: Nevo syndrome is allelic to the kyphoscoliotic type of the Ehlers-Danlos syndrome (EDS VIA). Am J Med Genet A. 2005 Mar 1;133A(2):158-64. [PubMed
]
- Walker LC, Overstreet MA, Siddiqui A, De Paepe A, Ceylaner G, Malfait F, Symoens S, Atsawasuwan P, Yamauchi M, Ceylaner S, Bank RA, Yeowell HN: A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient. J Invest Dermatol. 2005 May;124(5):914-8. [PubMed
]
- Giunta C, Randolph A, Steinmann B: Mutation analysis of the PLOD1 gene: an efficient multistep approach to the molecular diagnosis of the kyphoscoliotic type of Ehlers-Danlos syndrome (EDS VIA). Mol Genet Metab. 2005 Sep-Oct;86(1-2):269-76. Epub 2005 Jun 24. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5700 |
| Enzyme 10 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 |
| Enzyme 10 Synonyms |
- Lysyl hydroxylase 2
- LH2
|
| Enzyme 10 Gene Name |
PLOD2 |
| Enzyme 10 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAK
YFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAG
GPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIV
QQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARA
KNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSI
GVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIV
GPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTR
HGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERN
YFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDW
KEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRIS
GGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQ
RSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEG
LPVKNGTRYIAVSFIDP
|
| Enzyme 10 Number of Residues |
737 |
| Enzyme 10 Molecular Weight |
84685.1 |
| Enzyme 10 Theoretical pI |
6.69 |
| Enzyme 10 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 10 General Function |
Involved in oxidoreductase activity |
| Enzyme 10 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
2138314  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O00469  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PLOD2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>2214 bp
ATGGGGGGATGCACGGTGAAGCCTCAGCTGCTGCTCCTGGCGCTCGTCCTCCACCCCTGG
AATCCCTGTCTGGGTGCGGACTCGGAGAAGCCCTCGAGCATCCCCACAGATAAATTATTA
GTCATAACTGTAGCAACAAAAGAAAGTGATGGATTCCATCGATTTATGCAGTCAGCCAAA
TATTTCAATTATACTGTGAAGGTCCTTGGTCAAGGAGAAGAATGGAGAGGTGGTGATGGA
ATTAATAGTATTGGAGGGGGCCAGAAAGTGAGATTAATGAAAGAAGTCATGGAACACTAT
GCTGATCAAGATGATCTGGTTGTCATGTTTACTGAATGCTTTGATGTCATATTTGCTGGT
GGTCCAGAAGAAGTTCTAAAAAAATTCCAAAAGGCAAACCACAAAGTGGTCTTTGCAGCA
GATGGAATTTTGTGGCCAGATAAAAGACTAGCAGACAAGTATCCTGTTGTGCACATTGGG
AAACGCTATCTGAATTCAGGAGGATTTATTGGCTATGCTCCATATGTCAACCGTATAGTT
CAACAATGGAATCTCCAGGATAATGATGATGATCAGCTCTTTTACACTAAAGTTTACATT
GATCCACTGAAAAGGGAAGCTATTAACATCACATTGGATCACAAATGCAAAATTTTCCAG
ACCTTAAATGGAGCTGTAGATGAAGTTGTTTTAAAATTTGAAAATGGCAAAGCCAGAGCT
AAGAATACATTTTATGAAACATTACCAGTGGCAATTAATGGAAATGGACCCACCAAGATT
CTCCTGAATTATTTTGGAAACTATGTACCCAATTCATGGACACAGGATAATGGCTGCACT
CTTTGTGAATTCGATACAGTCGACTTGTCTGCAGTAGATGTCCATCCAAACGTATCAATA
GGTGTTTTTATTGAGCAACCAACCCCTTTTCTACCTCGGTTTCTGGACATATTGTTGACA
CTGGATTACCCAAAAGAAGCACTTAAACTTTTTATTCATAACAAAGAAGTTTATCATGAA
AAGGACATCAAGGTATTTTTTGATAAAGCTAAGCATGAAATCAAAACTATAAAAATAGTA
GGACCAGAAGAAAATCTAAGTCAAGCGGAAGCCAGAAACATGGGAATGGACTTTTGCCGT
CAGGATGAAAAGTGTGATTATTACTTTAGTGTGGATGCAGATGTTGTTTTGACAAATCCA
AGGACTTTAAAAATTTTGATTGAACAAAACAGAAAGATCATTGCTCCTCTTGTAACTCGT
CATGGAAAGCTGTGGTCCAATTTCTGGGGAGCATTGAGTCCTGATGGATACTATGCACGA
TCTGAAGATTATGTGGATATTGTTCAAGGGAATAGAGTAGGAGTATGGAATGTCCCATAT
ATGGCTAATGTGTACTTAATTAAAGGAAAGACACTCCGATCAGAGATGAATGAAAGGAAC
TATTTTGTTCGTGATAAACTGGATCCTGATATGGCTCTTTGCCGAAATGCTAGAGAAATG
GGTGTATTTATGTACATTTCTAATAGACATGAATTTGGAAGGCTATTATCCACTGCTAAT
TACAATACTTCCCATTATAACAATGACCTCTGGCAGATTTTTGAAAATCCTGTGGACTGG
AAGGAAAAGTATATAAACCGTGATTATTCAAAGATTTTCACTGAAAATATAGTTGAACAG
CCCTGTCCAGATGTCTTTTGGTTCCCCATATTTTCTGAAAAAGCCTGTGATGAATTGGTA
GAAGAAATGGAACATTACGGCAAATGGTCTGGGGGAAAACATCATGATAGCCGTATATCT
GGTGGTTATGAAAATGTCCCAACTGATGATATCCACATGAAGCAAGTTGATCTGGAGAAT
GTATGGCTTGATTTTATCCGGGAGTTCATTGCACCAGTTACACTGAAGGTCTTTGCAGGC
TATTATACGAAGGGATTTGCACTACTGAATTTTGTAGTAAAATACTCCCCTGAACGACAG
CGTTCTCTTCGTCCTCATCATGATGCTTCTACATTTACCATAAACATTGCACTTAATAAC
GTGGGAGAAGACTTTCAGGGAGGTGGTTGCAAATTTCTAAGGTACAATTGCTCTATTGAG
TCACCACGAAAAGGCTGGAGCTTCATGCATCCTGGGAGACTCACACATTTGCATGAAGGA
CTTCCTGTTAAAAATGGAACAAGATACATTGCAGTGTCATTTATAGATCCCTAA
|
| Enzyme 10 GenBank Gene ID |
U84573  |
| Enzyme 10 GeneCard ID |
PLOD2  |
| Enzyme 10 GenAtlas ID |
PLOD2  |
| Enzyme 10 HGNC ID |
HGNC:9082  |
| Enzyme 10 Chromosome Location |
3 |
| Enzyme 10 Locus |
3q23-q24 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Valtavaara M, Papponen H, Pirttila AM, Hiltunen K, Helander H, Myllyla R: Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J Biol Chem. 1997 Mar 14;272(11):6831-4. [PubMed
]
- Yeowell HN, Walker LC: Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 1999 Apr;18(2):179-87. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- van der Slot AJ, Zuurmond AM, Bardoel AF, Wijmenga C, Pruijs HE, Sillence DO, Brinckmann J, Abraham DJ, Black CM, Verzijl N, DeGroot J, Hanemaaijer R, TeKoppele JM, Huizinga TW, Bank RA: Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J Biol Chem. 2003 Oct 17;278(42):40967-72. Epub 2003 Jul 24. [PubMed
]
- Ha-Vinh R, Alanay Y, Bank RA, Campos-Xavier AB, Zankl A, Superti-Furga A, Bonafe L: Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2. Am J Med Genet A. 2004 Dec 1;131(2):115-20. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5701 |
| Enzyme 11 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 |
| Enzyme 11 Synonyms |
- Lysyl hydroxylase 3
- LH3
|
| Enzyme 11 Gene Name |
PLOD3 |
| Enzyme 11 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
|
| Enzyme 11 Number of Residues |
738 |
| Enzyme 11 Molecular Weight |
84784.5 |
| Enzyme 11 Theoretical pI |
5.95 |
| Enzyme 11 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 11 General Function |
Involved in oxidoreductase activity |
| Enzyme 11 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
3153235  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O60568  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PLOD3_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>2217 bp
ATGACCTCCTCGGGGCCTGGACCCCGGTTCCTGCTGCTGCTGCCGCTGCTGCTGCCCCCT
GCGGCCTCAGCCTCCGACCGGCCCCGGGGCCGAGACCCGGTCAACCCAGAGAAGCTGCTG
GTGATCACTGTGGCCACAGCTGAAACCGAGGGGTACCTGCGTTTCCTGCGCTCTGCGGAG
TTCTTCAACTACACTGTGCGGACCCTGGGCCTGGGAGAGGAGTGGCGAGGGGGTGATGTG
GCTCGAACAGTTGGTGGAGGACAGAAGGTCCGGTGGTTAAAGAAGGAAATGGAGAAATAC
GCTGACCGGGAGGATATGATCATCATGTTTGTGGATAGCTACGACGTGATTCTGGCCGGC
AGCCCCACAGAGCTGCTGAAGAAGTTCGTCCAGAGTGGCAGCCGCCTGCTCTTCTCTGCA
GAGAGCTTCTGCTGGCCCGAGTGGGGGCTGGCGGAGCAGTACCCTGAGGTGGGCACGGGG
AAGCGCTTCCTCAATTCTGGTGGATTCATCGGTTTTGCCACCACCATCCACCAAATCGTG
CGCCAGTGGAAGTACAAGGATGATGACGACGACCAGCTGTTCTACACACGGCTCTACCTG
GACCCAGGACTGAGGGAGAAACTCAGCCTTAATCTGGATCATAAGTCTCGGATCTTTCAG
AACCTCAACGGGGCTTTAGATGAAGTGGTTTTAAAGTTTGATCGGAACCGTGTGCGTATC
CGGAACGTGGCCTACGACACGCTCCCCATTGTGGTCCATGGAAACGGTCCCACTAAGCTG
CAGCTCAACTACCTGGGAAACTACGTCCCCAATGGCTGGACTCCTGAGGGAGGCTGTGGC
TTCTGCAACCAGGACCGGAGGACACTCCCGGGGGGGCAGCCTCCCCCCCGGGTGTTTCTG
GCCGTGTTTGTGGAACAGCCTACTCCGTTTCTGCCCCGCTTCCTGCAGCGGCTGCTACTC
CTGGACTATCCCCCCGACAGGGTCACCCTTTTCCTGCACAACAACGAGGTCTTCCATGAA
CCCCACATCGCTGACTCCTGGCCGCAGCTCCAGGACCACTTCTCAGCTGTGAAGCTCGTG
GGGCCGGAGGAGGCTCTGAGCCCAGGCGAGGCCAGGGACATGGCCATGGACCTGTGTCGG
CAGGACCCCGAGTGTGAGTTCTACTTCAGCCTGGACGCCGACGCTGTCCTCACCAACCTG
CAGACCCTGCGTATCCTCATTGAGGAGAACAGGAAGGTGATCGCCCCCATGCTGTCCCGC
CACGGCAAGCTGTGGTCCAACTTCTGGGGCGCCCTGAGCCCCGATGAGTACTACGCCCGC
TCCGAGGACTACGTGGAGCTGGTGCAGCGGAAGCGAGTGGGTGTGTGGAATGTACCATAC
ATCTCCCAGGCCTATGTGATCCGGGGTGATACCCTGCGGATGGAGCTGCCCCAGAGGGAT
GTGTTCTCGGGCAGTGACACAGACCCGGACATGGCCTTCTGTAAGAGCTTTCGAGACAAG
GGCATCTTCCTCCATCTGAGCAATCAGCATGAATTTGGCCGGCTCCTGGCCACTTCCAGA
TACGACACGGAGCACCTGCACCCCGACCTCTGGCAGATCTTCGACAACCCCGTCGACTGG
AAGGAGCAGTACATCCACGAGAACTACAGCCGGGCCCTGGAAGGGGAAGGAATCGTGGAG
CAGCCATGCCCGGACGTGTACTGGTTCCCACTGCTGTCAGAACAAATGTGTGATGAGCTG
GTGGCAGAGATGGAGCACTACGGCCAGTGGTCAGGCGGCCGGCATGAGGATTCAAGGCTG
GCTGGAGGCTACGAGAATGTGCCCACCGTGGACATCCACATGAAGCAGGTGGGGTACGAG
GACCAGTGGCTGCAGCTGCTGCGGACGTATGTGGGCCCCATGACCGAGAGCCTGTTTCCC
GGTTACCACACCAAGGCGCGGGCGGTGATGAACTTTGTGGTTCGCTACCGGCCAGACGAG
CAGCCGTCTCTGCGGCCACACCACGACTCATCCACCTTCACCCTCAACGTTGCCCTCAAC
CACAAGGGCCTGGACTATGAGGGAGGTGGCTGCCGCTTCCTGCGCTACGACTGTGTGATC
TCCTCCCCGAGGAAGGGCTGGGCACTCCTGCACCCCGGCCGCCTCACCCACTACCACGAG
GGGCTGCCAACGACCTGGGGCACACGCTACATCATGGTGTCCTTTGTCGACCCCTGA
|
| Enzyme 11 GenBank Gene ID |
AF046889  |
| Enzyme 11 GeneCard ID |
PLOD3  |
| Enzyme 11 GenAtlas ID |
PLOD3  |
| Enzyme 11 HGNC ID |
HGNC:9083  |
| Enzyme 11 Chromosome Location |
7 |
| Enzyme 11 Locus |
7q22 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Valtavaara M, Szpirer C, Szpirer J, Myllyla R: Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) J Biol Chem. 1998 May 22;273(21):12881-6. [PubMed
]
- Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10482-6. [PubMed
]
- Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI: Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). Matrix Biol. 2000 Feb;19(1):73-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Salo AM, Cox H, Farndon P, Moss C, Grindulis H, Risteli M, Robins SP, Myllyla R: A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene. Am J Hum Genet. 2008 Oct;83(4):495-503. Epub 2008 Oct 2. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5985 |
| Enzyme 12 Name |
Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial |
| Enzyme 12 Synonyms |
- 3-oxoacid-CoA transferase 1
- Somatic-type succinyl-CoA:3-oxoacid-CoA-transferase
- SCOT-s
|
| Enzyme 12 Gene Name |
OXCT1 |
| Enzyme 12 Protein Sequence |
>Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVL
VGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENA
EFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSV
AIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAET
TVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDD
VRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEAD
ADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMV
KGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDK
KKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN
|
| Enzyme 12 Number of Residues |
520 |
| Enzyme 12 Molecular Weight |
56157.2 |
| Enzyme 12 Theoretical pI |
7.52 |
| Enzyme 12 GO Classification |
| Function |
- CoA-transferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- catabolic process
- cellular catabolic process
- ketone body catabolic process
- metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 12 General Function |
Involved in CoA-transferase activity |
| Enzyme 12 Specific Function |
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate |
| Enzyme 12 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 12 Reactions |
- succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA [RN:R01780]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P55809  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
SCOT1_HUMAN  |
| Enzyme 12 PDB ID |
1OOY  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1563 bp
ATGGCGGCTCTCAAACTCCTCTCCTCCGGGCTTCGGCTCTGCGCCTCTGCCCGCGGATCT
GGGGCAACCTGGTACAAGGGATGTGTTTGTTCCTTTTCCACCAGTGCTCATCGCCATACC
AAGTTTTATACAGATCCAGTAGAAGCTGTAAAAGACATCCCTGATGGTGCCACGGTTTTG
GTTGGTGGTTTTGGGCTATGTGGAATTCCAGAGAATCTTATAGATGCTTTACTGAAAACT
GGAGTAAAAGGACTAACTGCAGTCAGCAACAATGCAGGGGTTGACAATTTTGGTTTGGGG
CTTTTGCTTCGGTCGAAGCAGATAAAACGCATGGTCTCTTCATATGTGGGAGAAAATGCA
GAATTTGAACGACAGTACTTATCTGGTGAATTAGAAGTGGAGCTGACACCACAGGGCACA
CTTGCAGAGAGGATCCGTGCAGGCGGGGCTGGAGTTCCTGCATTTTACACCCCAACAGGG
TATGGGACCCTGGTACAAGAAGGAGGATCGCCCATCAAATACAACAAAGATGGCAGTGTT
GCCATTGCCAGTAAGCCAAGAGAGGTGAGGGAGTTCAATGGTCAGCACTTTATTTTGGAG
GAAGCAATTACAGGGGATTTTGCTTTGGTGAAAGCCTGGAAGGCGGACCGAGCAGGAAAC
GTGATTTTCAGGAAAAGTGCAAGGAATTTCAACTTGCCAATGTGCAAAGCTGCAGAAACC
ACAGTGGTAGAGGTTGAAGAAATTGTGGATATTGGAGCATTTGCTCCAGAAGACATCCAT
ATTCCTCAGATTTATGTACATCGCCTTATAAAGGGAGAAAAATATGAGAAAAGAATTGAG
CGTTTATCAATCCGGAAAGAGGGAGATGGGGAAGCCAAATCTGCTAAACCTGGAGATGAC
GTAAGGGAACGAATCATCAAGAGGGCCGCTCTTGAGTTTGAGGATGGCATGTATGCTAAT
TTGGGCATAGGAATCCCTCTCCTGGCCAGCAATTTTATCAGCCCAAATATAACTGTTCAT
CTTCAAAGTGAAAATGGAGTTCTGGGTTTGGGTCCATATCCACGACAACATGAAGCTGAT
GCAGATCTCATCAATGCAGGCAAGGAAACAGTTACTATTCTTCCAGGAGCCTCTTTTTTC
TCCAGCGATGAATCATTTGCAATGATTAGAGGTGGACACGTCGATCTGACAATGCTAGGA
GCGATGCAGGTTTCCAAATATGGTGACCTGGCTAACTGGATGATACCTGGGAAGATGGTG
AAAGGAATGGGAGGTGCTATGGATTTAGTGTCCAGTGCGAAAACCAAAGTGGTGGTCACC
ATGGAGCATTCTGCAAAGGGAAATGCACATAAAATCATGGAGAAATGTACATTACCATTG
ACTGGAAAGCAATGTGTCAACCGCATTATTACTGAAAAGGCTGTGTTTGATGTGGACAAG
AAGAAAGGGTTGACTCTGATTGAGCTCTGGGAAGGCCTGACAGTGGATGACGTACAAAAG
AGTACTGGGTGTGATTTTGCAGTTTCACCAAAACTCATGCCAATGCAGCAGATCGCAAAT
TGA
|
| Enzyme 12 GenBank Gene ID |
U62961  |
| Enzyme 12 GeneCard ID |
OXCT1  |
| Enzyme 12 GenAtlas ID |
OXCT1  |
| Enzyme 12 HGNC ID |
HGNC:8527  |
| Enzyme 12 Chromosome Location |
5 |
| Enzyme 12 Locus |
5p13.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Kassovska-Bratinova S, Fukao T, Song XQ, Duncan AM, Chen HS, Robert MF, Perez-Cerda C, Ugarte M, Chartrand C, Vobecky S, Kondo N, Mitchell GA: Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient. Am J Hum Genet. 1996 Sep;59(3):519-28. [PubMed
]
- Fukao T, Mitchell GA, Song XQ, Nakamura H, Kassovska-Bratinova S, Orii KE, Wraith JE, Besley G, Wanders RJ, Niezen-Koning KE, Berry GT, Palmieri M, Kondo N: Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations. Genomics. 2000 Sep 1;68(2):144-51. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Song XQ, Fukao T, Watanabe H, Shintaku H, Hirayama K, Kassovska-Bratinova S, Kondo N, Mitchell GA: Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings. Hum Mutat. 1998;12(2):83-8. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5988 |
| Enzyme 13 Name |
Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial |
| Enzyme 13 Synonyms |
- 3-oxoacid-CoA transferase 2A
- Testis-specific succinyl-CoA:3-oxoacid CoA-transferase
- SCOT-t
|
| Enzyme 13 Gene Name |
OXCT2 |
| Enzyme 13 Protein Sequence |
>Succinyl-CoA:3-ketoacid-coenzyme A transferase 2, mitochondrial
MAALRLLASVLGRGVPAGGSGLALSQGCARCFATSPRLRAKFYADPVEMVKDISDGATVM
IGGFGLCGIPENLIAALLRTRVKDLQVVSSNVGVEDFGLGLLLAARQVRRIVCSYVGENT
LCESQYLAGELELELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGAPIRYTPDGHL
ALMSQPREVREFNGDHFLLERAIRADFALVKGWKADRAGNVVFRRSARNFNVPMCKAADV
TAVEVEEIVEVGAFPPEDIHVPNIYVDRVIKGQKYEKRIERLTILKEEDGDAGKEEDART
RIIRRAALEFEDGMYANLGIGIPLLASNFISPSMTVHLHSENGILGLGPFPTEDEVDADL
INAGKQTVTVLPGGCFFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMIPGKKVKGM
GGAMDLVSSQKTRVVVTMQHCTKDNTPKIMEKCTMPLTGKRCVDRIITEKAVFDVHRKKE
LTLRELWEGLTVDDIKKSTGCAFAVSPNLRPMQQVAP
|
| Enzyme 13 Number of Residues |
517 |
| Enzyme 13 Molecular Weight |
56139.4 |
| Enzyme 13 Theoretical pI |
7.15 |
| Enzyme 13 GO Classification |
| Function |
- CoA-transferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- catabolic process
- cellular catabolic process
- ketone body catabolic process
- metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 13 General Function |
Involved in CoA-transferase activity |
| Enzyme 13 Specific Function |
Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate |
| Enzyme 13 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 13 Reactions |
- succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA [RN:R01780]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
Not Available |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9BYC2  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
SCOT2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1554 bp
ATGGCGGCGCTGCGGCTCCTGGCGTCAGTGCTCGGGCGCGGGGTCCCCGCCGGCGGCTCA
GGGCTCGCGCTGTCCCAGGGCTGCGCCCGCTGCTTTGCCACCAGTCCCCGGCTCCGTGCC
AAGTTCTACGCGGACCCGGTGGAGATGGTGAAGGACATCTCTGACGGGGCGACCGTCATG
ATCGGGGGCTTCGGGCTCTGCGGGATCCCCGAGAACCTGATCGCCGCGCTGCTCAGGACC
CGCGTGAAAGACCTGCAGGTGGTCAGCAGCAACGTGGGCGTGGAGGACTTCGGCCTGGGC
CTCCTGCTGGCCGCCAGGCAGGTCCGTCGCATCGTCTGTTCCTACGTGGGCGAGAACACC
CTGTGCGAGAGCCAGTACCTGGCAGGAGAGCTGGAGCTGGAGCTCACGCCCCAGGGCACC
CTGGCCGAGCGCATCCGCGCGGGGGGCGCCGGGGTGCCCGCCTTCTACACCCCCACGGGC
TACGGGACCCTGGTCCAGGAAGGGGGCGCCCCCATCCGCTACACCCCGGACGGCCACCTG
GCGCTCATGAGCCAGCCCCGAGAGGTGAGGGAGTTCAACGGCGACCACTTCCTTTTGGAG
CGCGCCATCCGGGCAGACTTCGCCCTGGTGAAAGGGTGGAAGGCCGACCGGGCAGGAAAC
GTGGTCTTCAGGAGAAGCGCCCGCAATTTCAACGTGCCCATGTGCAAAGCTGCAGACGTC
ACGGCGGTGGAGGTGGAAGAGATCGTGGAGGTGGGGGCTTTCCCCCCAGAAGACATCCAC
GTTCCTAACATTTATGTAGATCGCGTGATAAAGGGGCAGAAATACGAGAAACGAATTGAG
CGCTTAACGATCCTGAAAGAGGAAGATGGAGACGCTGGAAAGGAAGAGGACGCCAGGACG
CGCATCATCAGACGCGCAGCTCTGGAATTTGAGGACGGCATGTACGCCAATCTGGGCATA
GGCATCCCCCTGCTGGCCAGCAACTTCATCAGTCCCAGCATGACTGTCCATCTTCACAGT
GAGAACGGGATCCTGGGCCTGGGCCCGTTTCCCACGGAAGATGAGGTGGATGCCGACCTC
ATCAATGCAGGCAAGCAGACGGTCACGGTGCTTCCCGGGGGCTGCTTCTTCGCCAGCGAC
GACTCCTTCGCCATGATCCGAGGGGGACACATCCAACTAACCATGCTTGGAGCCATGCAG
GTTTCCAAATACGGCGACCTGGCGAACTGGATGATCCCTGGCAAGAAGGTGAAAGGCATG
GGCGGTGCCATGGACTTGGTGTCCAGTCAGAAGACCAGAGTGGTGGTCACCATGCAGCAC
TGCACAAAGGACAACACCCCCAAGATCATGGAGAAATGCACCATGCCGCTGACCGGGAAG
CGGTGCGTGGACCGCATCATCACCGAGAAGGCCGTGTTTGACGTGCACAGGAAGAAAGAG
CTGACGCTGAGGGAGCTCTGGGAGGGCCTGACGGTGGACGACATCAAAAAGAGCACGGGG
TGTGCCTTTGCTGTGTCCCCGAACCTCAGGCCCATGCAGCAGGTGGCACCCTGA
|
| Enzyme 13 GenBank Gene ID |
AB050193  |
| Enzyme 13 GeneCard ID |
OXCT2  |
| Enzyme 13 GenAtlas ID |
OXCT2  |
| Enzyme 13 HGNC ID |
HGNC:18606  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p34 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Tanaka H, Kohroki J, Iguchi N, Onishi M, Nishimune Y: Cloning and characterization of a human orthologue of testis-specific succinyl CoA: 3-oxo acid CoA transferase (Scot-t) cDNA. Mol Hum Reprod. 2002 Jan;8(1):16-23. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6171 |
| Enzyme 14 Name |
Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial |
| Enzyme 14 Synonyms |
- Succinyl-CoA synthetase subunit alpha
- SCS-alpha
|
| Enzyme 14 Gene Name |
SUCLG1 |
| Enzyme 14 Protein Sequence |
>Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
MTATLAAAADIATMVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIIC
QGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYV
PPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGE
CKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCL
EIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHA
GAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
|
| Enzyme 14 Number of Residues |
346 |
| Enzyme 14 Molecular Weight |
36249.5 |
| Enzyme 14 Theoretical pI |
9.04 |
| Enzyme 14 GO Classification |
| Function |
- ATP citrate synthase activity
- CoA-ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- succinate-CoA ligase (ADP-forming) activity
- succinate-CoA ligase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in catalytic activity |
| Enzyme 14 Specific Function |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
109452591  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P53597  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
SUCA_HUMAN  |
| Enzyme 14 PDB ID |
1EUC  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1041 bp
ATGACCGCAACCCTTGCCGCTGCCGCTGACATCGCTACCATGGTCTCCGGCAGCAGCGGC
CTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTGCCGCAGAATGGAATTCGGCAT
TGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGATAAAAATACAAAGATTATTTGC
CAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAGCAGGCATTGGAATATGGCACC
AAACTCGTTGGAGGAACCACTCCAGGGAAAGGAGGCCAGACACATCTGGGCTTACCTGTC
TTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCAACGGCTTCTGTCATTTATGTT
CCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATTGAGGCAGAAATTCCCTTGGTT
GTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTACGAGTCAAGCACAAACTGCTG
CGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCTGGAGTCATCAATCCTGGAGAA
TGTAAAATTGGCATCATGCCTGGCCATATTCACAAAAAAGGAAGGATTGGCATTGTGTCC
AGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACAACGCAAGTTGGATTGGGGCAG
TCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGAACAGATTTTATTGACTGCCTC
GAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATATTGATTGGTGAAATTGGTGGT
AATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACATAATTCAGGTCCAAATTCCAAG
CCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCTGGGAGAAGAATGGGTCATGCC
GGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAGAAGATCTCTGCCCTTCAGAGT
GCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGAACCACGATCTACAAGGAATTT
GAAAAGAGGAAGATGCTATGA
|
| Enzyme 14 GenBank Gene ID |
NM_003849.3  |
| Enzyme 14 GeneCard ID |
SUCLG1  |
| Enzyme 14 GenAtlas ID |
SUCLG1  |
| Enzyme 14 HGNC ID |
HGNC:11449  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2p11.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed
]
- Ostergaard E, Christensen E, Kristensen E, Mogensen B, Duno M, Shoubridge EA, Wibrand F: Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion. Am J Hum Genet. 2007 Aug;81(2):383-7. Epub 2007 Jun 4. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6173 |
| Enzyme 15 Name |
Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial |
| Enzyme 15 Synonyms |
- GTP-specific succinyl-CoA synthetase subunit beta
- Succinyl-CoA synthetase beta-G chain
- SCS-betaG
|
| Enzyme 15 Gene Name |
SUCLG2 |
| Enzyme 15 Protein Sequence |
>Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
|
| Enzyme 15 Number of Residues |
432 |
| Enzyme 15 Molecular Weight |
46510.2 |
| Enzyme 15 Theoretical pI |
6.18 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- purine nucleoside binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in catalytic activity |
| Enzyme 15 Specific Function |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
157779135  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q96I99  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SUCB2_HUMAN  |
| Enzyme 15 PDB ID |
1EUC  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1299 bp
ATGGCGTCCCCCGTAGCAGCGCAGGCCGGGAAGCTTCTGCGAGCCCTAGCGCTGCGGCCC
CGCTTCCTGGCGGCCGGGTCCCAGGCAGTTCAATTAACCTCCAGAAGATGGCTGAACCTG
CAGGAATACCAGAGCAAGAAACTGATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTT
GTAGCAGACACTGCAAATGAAGCTCTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATT
GTTTTAAAAGCCCAGATCTTAGCTGGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTG
AAAGGAGGTGTTCATTTAACAAAAGACCCTAATGTTGTGGGACAGCTGGCTAAACAGATG
ATTGGGTACAATCTAGCGACAAAACAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTG
ATGGTTGCTGAAGCCTTGGATATTTCCAGAGAAACCTACCTGGCAATTCTGATGGACCGG
TCCTGCAATGGCCCCGTGCTGGTGGGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTG
GCTGCTTCAAACCCGGAGCTCATTTTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAG
GACAGCCAAGCTCAGCGGATGGCCGAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAG
GCTGCAGATCAAATTACGAAGCTGTATAATCTCTTCCTGAAAATTGATGCTACTCAGGTG
GAAGTGAATCCCTTTGGTGAAACTCCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATA
AACTTTGATGACAACGCAGAATTCCGACAAAAAGACATATTTGCTATGGACGACAAATCA
GAGAATGAGCCCATTGAAAATGAAGCTGCCAAATATGATCTAAAATACATAGGACTAGAT
GGGAACATTGCCTGCTTTGTGAATGGTGCTGGGCTCGCCATGGCTACTTGTGATATCATT
TTCCTTAATGGTGGGAAGCCAGCCAACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCT
CAAGTATATCAAGCATTCAAATTGCTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTC
AATATATTTGGTGGTATCGTCAACTGTGCCATCATTGCCAATGGGATCACCAAAGCCTGC
CGGGAGCTAGAACTCAAGGTGCCCCTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAG
GCCCAGAAGATACTCAACAACAGCGGACTCCCCATTACTTCAGCCATTGACCTGGAGGAT
GCAGCCAAGAAGGCTGTGGCCAGTGTGGCCAAGAAGTGA
|
| Enzyme 15 GenBank Gene ID |
NM_003848.3  |
| Enzyme 15 GeneCard ID |
SUCLG2  |
| Enzyme 15 GenAtlas ID |
SUCLG2  |
| Enzyme 15 HGNC ID |
HGNC:11450  |
| Enzyme 15 Chromosome Location |
3 |
| Enzyme 15 Locus |
3p14.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6259 |
| Enzyme 16 Name |
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial |
| Enzyme 16 Synonyms |
- ATP-specific succinyl-CoA synthetase subunit beta
- Renal carcinoma antigen NY-REN-39
- Succinyl-CoA synthetase beta-A chain
- SCS-betaA
|
| Enzyme 16 Gene Name |
SUCLA2 |
| Enzyme 16 Protein Sequence |
>Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
|
| Enzyme 16 Number of Residues |
463 |
| Enzyme 16 Molecular Weight |
50316.9 |
| Enzyme 16 Theoretical pI |
7.50 |
| Enzyme 16 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- purine nucleoside binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in catalytic activity |
| Enzyme 16 Specific Function |
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- ATP + succinate + CoA = ADP + phosphate + succinyl-CoA [RN:R00405]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9P2R7  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
SUCB1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1392 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA
|
| Enzyme 16 GenBank Gene ID |
AB035863  |
| Enzyme 16 GeneCard ID |
SUCLA2  |
| Enzyme 16 GenAtlas ID |
SUCLA2  |
| Enzyme 16 HGNC ID |
HGNC:11448  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
13q12.2-q13.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Furuyama K, Sassa S: Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000 Mar;105(6):757-64. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed
]
- Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Elpeleg O, Miller C, Hershkovitz E, Bitner-Glindzicz M, Bondi-Rubinstein G, Rahman S, Pagnamenta A, Eshhar S, Saada A: Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion. Am J Hum Genet. 2005 Jun;76(6):1081-6. Epub 2005 Apr 22. [PubMed
]
- Ostergaard E, Hansen FJ, Sorensen N, Duno M, Vissing J, Larsen PL, Faeroe O, Thorgrimsson S, Wibrand F, Christensen E, Schwartz M: Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused by SUCLA2 mutations. Brain. 2007 Mar;130(Pt 3):853-61. Epub 2007 Feb 7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Carrozzo R, Dionisi-Vici C, Steuerwald U, Lucioli S, Deodato F, Di Giandomenico S, Bertini E, Franke B, Kluijtmans LA, Meschini MC, Rizzo C, Piemonte F, Rodenburg R, Santer R, Santorelli FM, van Rooij A, Vermunt-de Koning D, Morava E, Wevers RA: SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness. Brain. 2007 Mar;130(Pt 3):862-74. Epub 2007 Feb 14. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6310 |
| Enzyme 17 Name |
Aspartyl/asparaginyl beta-hydroxylase |
| Enzyme 17 Synonyms |
- Aspartate beta-hydroxylase
- ASP beta-hydroxylase
- Peptide-aspartate beta-dioxygenase
|
| Enzyme 17 Gene Name |
ASPH |
| Enzyme 17 Protein Sequence |
>Aspartyl/asparaginyl beta-hydroxylase
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMV
IALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVP
PEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQ
QEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSE
PVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSI
FPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEA
VNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLK
LSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEV
LSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGN
KEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDE
GLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGC
RRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFD
DSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
|
| Enzyme 17 Number of Residues |
758 |
| Enzyme 17 Molecular Weight |
85862.1 |
| Enzyme 17 Theoretical pI |
4.65 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptide-aspartate beta-dioxygenase activity
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- oxidation reduction
- peptidyl-amino acid modification
- protein modification process
|
| Component |
- cell part
- integral to endoplasmic reticulum membrane
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane
- membrane part
|
|
| Enzyme 17 General Function |
Involved in peptide-aspartate beta-dioxygenase activity |
| Enzyme 17 Specific Function |
Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
- peptide-L-aspartate + 2-oxoglutarate + O2 = peptide-3-hydroxy-L-aspartate + succinate + CO2 [RN:R04073]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
14589866  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q12797  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
ASPH_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>2277 bp
ATGGCCCAGCGTAAGAATGCCAAGAGCAGCGGCAACAGCAGCAGCAGCGGCTCCGGCAGC
GGTAGCACGAGTGCGGGCAGCAGCAGCCCCGGGGCCCGGAGAGAGACAAAGCATGGAGGA
CACAAGAATGGGAGGAAAGGCGGACTCTCAGGAACTTCATTCTTCACGTGGTTTATGGTG
ATTGCATTGCTGGGCGTCTGGACATCTGTAGCTGTCGTTTGGTTTGATCTTGTTGACTAT
GAGGAAGTTCTAGGAAAACTAGGAATCTATGATGCTGATGGTGATGGAGATTTTGATGTG
GATGATGCCAAAGTTTTATTAGGACTTAAAGAGAGATCTACTTCAGAGCCAGCAGTCCCG
CCAGAAGAGGCTGAGCCACACACTGAGCCCGAGGAGCAGGTTCCTGTGGAGGCAGAACCC
CAGAATATCGAAGATGAAGCAAAAGAACAAATTCAGTCCCTTCTCCATGAAATGGTACAC
GCAGAACATGTTGAGGGAGAAGACTTGCAACAAGAAGATGGACCCACAGGAGAACCACAA
CAAGAGGATGATGAGTTTCTTATGGCGACTGATGTAGATGATAGATTTGAGACCCTGGAA
CCTGAAGTATCTCATGAAGAAACCGAGCATAGTTACCACGTGGAAGAGACAGTTTCACAA
GACTGTAATCAGGATATGGAAGAGATGATGTCTGAGCAGGAAAATCCAGATTCCAGTGAA
CCAGTAGTAGAAGATGAAAGATTGCACCATGATACAGATGATGTAACATACCAAGTCTAT
GAGGAACAAGCAGTATATGAACCTCTAGAAAATGAAGGGATAGAAATCACAGAAGTAACT
GCTCCCCCTGAGGATAATCCTGTAGAAGATTCACAGGTAATTGTAGAAGAAGTAAGCATT
TTTCCTGTGGAAGAACAGCAGGAAGTACCACCAGAAACAAATAGAAAAACAGATGATCCA
GAACAAAAAGCAAAAGTTAAGAAAAAGAAGCCTAAACTTTTAAATAAATTTGATAAGACT
ATTAAAGCTGAACTTGATGCTGCAGAAAAACTCCGTAAAAGGGGAAAAATTGAGGAAGCA
GTGAATGCATTTAAAGAACTAGTACGCAAATACCCTCAGAGTCCACGAGCAAGATATGGG
AAGGCGCAGTGTGAGGATGATTTGGCTGAGAAGAGGAGAAGTAATGAGGTGCTACGTGGA
GCCATCGAGACCTACCAAGAGGTGGCCAGCCTACCTGATGTCCCTGCAGACCTGCTGAAG
CTGAGTTTGAAGCGTCGCTCAGACAGGCAACAATTTCTAGGTCATATGAGAGGTTCCCTG
CTTACCCTGCAGAGATTAGTTCAACTATTTCCCAATGATACTTCCTTAAAAAATGACCTT
GGCGTGGGATACCTCTTGATAGGAGATAATGACAATGCAAAGAAAGTTTATGAAGAGGTG
CTGAGTGTGACACCTAATGATGGCTTTGCTAAAGTCCATTATGGCTTCATCCTGAAGGCA
CAGAACAAAATTGCTGAGAGCATCCCATATTTAAAGGAAGGAATAGAATCCGGAGATCCT
GGCACTGATGATGGGAGATTTTATTTCCACCTGGGGGATGCCATGCAGAGGGTTGGGAAC
AAAGAGGCATATAAGTGGTATGAGCTTGGGCACAAGAGAGGACACTTTGCATCTGTCTGG
CAACGCTCACTCTACAATGTGAATGGACTGAAAGCACAGCCTTGGTGGACCCCAAAAGAA
ACGGGCTACACAGAGTTAGTAAAGTCTTTAGAAAGAAACTGGAAGTTAATCCGAGATGAA
GGCCTTGCAGTGATGGATAAAGCCAAAGGTCTCTTCCTGCCTGAGGATGAAAACCTGAGG
GAAAAAGGGGACTGGAGCCAGTTCACGCTGTGGCAGCAAGGAAGAAGAAATGAAAATGCC
TGCAAAGGAGCTCCTAAAACCTGTACCTTACTAGAAAAGTTCCCCGAGACAACAGGATGC
AGAAGAGGACAGATCAAATATTCCATCATGCACCCCGGGACTCACGTGTGGCCGCACACA
GGGCCCACAAACTGCAGGCTCCGAATGCACCTGGGCTTGGTGATTCCCAAGGAAGGCTGC
AAGATTCGATGTGCCAACGAGACCAAGACCTGGGAGGAAGGCAAGGTGCTCATCTTTGAT
GACTCCTTTGAGCACGAGGTATGGCAGGATGCCTCATCTTTCCGGCTGATATTCATCGTG
GATGTGTGGCATCCGGAACTGACACCACAGCAGAGACGCAGCCTTCCAGCAATTTAG
|
| Enzyme 17 GenBank Gene ID |
NM_004318.3  |
| Enzyme 17 GeneCard ID |
ASPH  |
| Enzyme 17 GenAtlas ID |
ASPH  |
| Enzyme 17 HGNC ID |
HGNC:757  |
| Enzyme 17 Chromosome Location |
8 |
| Enzyme 17 Locus |
8q12.1 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Korioth F, Gieffers C, Frey J: Cloning and characterization of the human gene encoding aspartyl beta-hydroxylase. Gene. 1994 Dec 15;150(2):395-9. [PubMed
]
- Lavaissiere L, Jia S, Nishiyama M, de la Monte S, Stern AM, Wands JR, Friedman PA: Overexpression of human aspartyl(asparaginyl)beta-hydroxylase in hepatocellular carcinoma and cholangiocarcinoma. J Clin Invest. 1996 Sep 15;98(6):1313-23. [PubMed
]
- Lim KY, Hong CS, Kim DH: cDNA cloning and characterization of human cardiac junctin. Gene. 2000 Sep 5;255(1):35-42. [PubMed
]
- Dinchuk JE, Henderson NL, Burn TC, Huber R, Ho SP, Link J, O'Neil KT, Focht RJ, Scully MS, Hollis JM, Hollis GF, Friedman PA: Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin. J Biol Chem. 2000 Dec 15;275(50):39543-54. [PubMed
]
- Wetzel GT, Ding S, Chen F: Molecular cloning of junctin from human and developing rabbit heart. Mol Genet Metab. 2000 Mar;69(3):252-8. [PubMed
]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6311 |
| Enzyme 18 Name |
Hypoxia-inducible factor 1-alpha inhibitor |
| Enzyme 18 Synonyms |
- Factor inhibiting HIF-1
- FIH-1
- Hypoxia-inducible factor asparagine hydroxylase
|
| Enzyme 18 Gene Name |
HIF1AN |
| Enzyme 18 Protein Sequence |
>Hypoxia-inducible factor 1-alpha inhibitor
MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEE
PVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNR
EEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWG
QLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGA
PTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
|
| Enzyme 18 Number of Residues |
349 |
| Enzyme 18 Molecular Weight |
40285.2 |
| Enzyme 18 Theoretical pI |
5.28 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Involved in metal ion binding |
| Enzyme 18 Specific Function |
Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300- interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
- peptide-L-aspartate + 2-oxoglutarate + O2 = peptide-3-hydroxy-L-aspartate + succinate + CO2 [RN:R04073]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9NWT6  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
HIF1N_HUMAN  |
| Enzyme 18 PDB ID |
1H2N  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1050 bp
ATGGCGGCGACAGCGGCGGAGGCTGTGGCCTCTGGCTCTGGAGAGCCCCGGGAGGAGGCT
GGAGCCCTCGGCCCCGCCTGGGATGAATCCCAGTTGCGCAGTTATAGCTTCCCGACTAGG
CCCATTCCGCGTCTGAGTCAGAGCGACCCCCGGGCAGAGGAGCTTATTGAGAATGAGGAG
CCTGTGGTGCTGACCGACACAAATCTTGTGTATCCTGCCCTGAAATGGGACCTTGAATAC
CTGCAAGAGAATATTGGCAATGGAGACTTCTCTGTGTACAGTGCCAGCACCCACAAGTTC
TTGTACTATGATGAGAAGAAGATGGCCAATTTCCAGAACTTTAAGCCGAGGTCCAACAGG
GAAGAAATGAAATTTCATGAGTTCGTTGAGAAACTGCAGGATATACAGCAGCGAGGAGGG
GAAGAGAGGTTGTATCTGCAGCAAACGCTCAATGACACTGTGGGCAGGAAGATTGTCATG
GACTTCTTAGGTTTTAACTGGAACTGGATTAATAAGCAACAGGGAAAGCGTGGCTGGGGG
CAGCTTACCTCTAACCTGCTGCTCATTGGCATGGAAGGAAATGTGACACCTGCTCACTAT
GATGAGCAGCAGAACTTTTTTGCTCAGATAAAAGGTTACAAACGATGCATCTTATTCCCT
CCGGATCAGTTCGAGTGCCTCTACCCATACCCTGTTCATCACCCATGTGACAGACAGAGC
CAGGTGGACTTTGACAATCCCGACTACGAGAGGTTCCCTAATTTCCAAAATGTGGTTGGT
TACGAAACAGTGGTTGGCCCTGGTGATGTTCTTTACATCCCAATGTACTGGTGGCATCAC
ATAGAGTCATTACTAAATGGGGGGATTACCATCACTGTGAACTTCTGGTATAAGGGGGCT
CCCACCCCTAAGAGAATTGAATATCCTCTCAAAGCTCATCAGAAAGTGGCCATAATGAGA
AACATTGAGAAGATGCTTGGAGAGGCCTTGGGGAACCCACAAGAGGTGGGGCCCTTGTTG
AACACAATGATCAAGGGCCGATACAACTAG
|
| Enzyme 18 GenBank Gene ID |
AF395830  |
| Enzyme 18 GeneCard ID |
HIF1AN  |
| Enzyme 18 GenAtlas ID |
HIF1AN  |
| Enzyme 18 HGNC ID |
HGNC:17113  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
10q24 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Mahon PC, Hirota K, Semenza GL: FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 2001 Oct 15;15(20):2675-86. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK: FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 2002 Jun 15;16(12):1466-71. [PubMed
]
- Hewitson KS, McNeill LA, Riordan MV, Tian YM, Bullock AN, Welford RW, Elkins JM, Oldham NJ, Bhattacharya S, Gleadle JM, Ratcliffe PJ, Pugh CW, Schofield CJ: Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family. J Biol Chem. 2002 Jul 19;277(29):26351-5. Epub 2002 May 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Dann CE 3rd, Bruick RK, Deisenhofer J: Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15351-6. Epub 2002 Nov 13. [PubMed
]
- Elkins JM, Hewitson KS, McNeill LA, Seibel JF, Schlemminger I, Pugh CW, Ratcliffe PJ, Schofield CJ: Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. J Biol Chem. 2003 Jan 17;278(3):1802-6. Epub 2002 Nov 21. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6912 |
| Enzyme 19 Name |
Mitochondrial dicarboxylate carrier |
| Enzyme 19 Synonyms |
- Solute carrier family 25 member 10
|
| Enzyme 19 Gene Name |
SLC25A10 |
| Enzyme 19 Protein Sequence |
>Mitochondrial dicarboxylate carrier
MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILAL
YSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPA
DLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLS
CYDQAKQLVLSTGYLSDNIFTHFVASFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHC
AVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS
|
| Enzyme 19 Number of Residues |
287 |
| Enzyme 19 Molecular Weight |
31282.2 |
| Enzyme 19 Theoretical pI |
9.91 |
| Enzyme 19 GO Classification |
| Function |
|
| Process |
- establishment of localization
- intracellular transport
- mitochondrial transport
- transmembrane transport
- transport
|
| Component |
- cell part
- intracellular membrane-bounded organelle
- membrane
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 19 General Function |
Involved in binding |
| Enzyme 19 Specific Function |
Involved in translocation of malonate, malate and succinate in exchange for phosphate, sulfate, sulfite or thiosulfate across mitochondrial inner membrane |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
- 10-30
63-82
103-123
163-182
203-223
255-275
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
6179584  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9UBX3  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
DIC_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>864 bp
ATGGCAGCCGAGGCGCGCGTGTCGCGCTGGTACTTCGGGGGGCTGGCCTCCTGCGGGGCC
GCCTGCTGCACGCACCCGCTGGACCTGCTCAAGGTGCATCTGCAGACGCAGCAGGAGGTG
AAGCTGCGCATGACGGGCATGGCGCTGCGGGTGGTGCGTACCGACGGCATCCTGGCACTC
TACAGCGGCCTGAGCGCCTCGCTGTGCAGACAGATGACCTACTCCCTGACTCGGTTCGCC
ATCTACGAGACTGTGCGGGACCGCGTGGCCAAGGGCAGCCAGGGGCCTCTCCCCTTCCAC
GAGAAGGTGTTGCTGGGCTCCGTCAGCGGTTTAGCTGGAGGCTTCGTGGGGACGCCCGCA
GACTTGGTCAACGTCAGGATGCAGAACGACGTGAAGCTGCCCCAGGGTCAGCGGCGCAAC
TACGCCCATGCGCTGGATGGCCTGTACCGCGTAGCTCGTGAAGAGGGTCTCAGGAGACTG
TTCTCGGGTGCAACCATGGCATCCAGCCGAGGGGCCTTAGTCACTGTGGGCCAGCTGTCC
TGCTACGACCAGGCCAAGCAGCGGGTCCTTAGCACCGGGTACCTCTCTGACAACATCTTC
ACTCACTTTGTCGCCAGCTTTATTGCAGGTGGATGTGCCACGTTCCTGTGCCAGCCCCTG
GATGTGCTGAAGACTCGCCTGATGAACTCCAAGGGGGAGTATCAGGGCGTTTTCCACTGC
GCCGTGGAGACAGCGAAGCTCGGGCCTCTGGCCTTTTACAAGGGCCTCGTCCCAGCTGGC
ATCCGCCTCATCCCCCACACCGTGCTCACTTTTGTGTTTCTGGAACAGCTACGCAAAAAC
TTTGGCATCAAAGTGCCATCCTGA
|
| Enzyme 19 GenBank Gene ID |
AJ131613  |
| Enzyme 19 GeneCard ID |
SLC25A10  |
| Enzyme 19 GenAtlas ID |
SLC25A10  |
| Enzyme 19 HGNC ID |
HGNC:10980  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
17q25.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Fiermonte G, Dolce V, Arrigoni R, Runswick MJ, Walker JE, Palmieri F: Organization and sequence of the gene for the human mitochondrial dicarboxylate carrier: evolution of the carrier family. Biochem J. 1999 Dec 15;344 Pt 3:953-60. [PubMed
]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
7930 |
| Enzyme 20 Name |
Solute carrier family 13 member 3 |
| Enzyme 20 Synonyms |
- Na(+)/dicarboxylate cotransporter 3
- NaDC-3
- hNaDC3
- Sodium-dependent high-affinity dicarboxylate transporter 2
|
| Enzyme 20 Gene Name |
SLC13A3 |
| Enzyme 20 Protein Sequence |
>Solute carrier family 13 member 3
MAALAAAAKKVWSARRLLVLLFTPLALLPVVFALPPKEGRCLFVILLMAVYWCTEALPLS
VTALLPIVLFPFMGILPSNKVCPQYFLDTNFLFLSGLIMASAIEEWNLHRRIALKILMLV
GVQPARLILGMMVTTSFLSMWLSNTASTAMMLPIANAILKSLFGQKEVRKDPSQESEENT
AAVRRNGLHTVPTEMQFLASTEAKDHPGETEVPLDLPADSRKEDEYRRNIWKGFLISIPY
SASIGGTATLTGTAPNLILLGQLKSFFPQCDVVNFGSWFIFAFPLMLLFLLAGWLWISFL
YGGLSFRGWRKNKSEIRTNAEDRARAVIREEYQNLGPIKFAEQAVFILFCMFAILLFTRD
PKFIPGWASLFNPGFLSDAVTGVAIVTILFFFPSQRPSLKWWFDFKAPNTETEPLLTWKK
AQETVPWNIILLLGGGFAMAKGCEESGLSVWIGGQLHPLENVPPALAVLLITVVIAFFTE
FASNTATIIIFLPVLAELAIRLRVHPLYLMIPGTVGCSFAFMLPVSTPPNSIAFASGHLL
VKDMVRTGLLMNLMGVLLLSLAMNTWAQTIFQLGTFPDWADMYSVNVTALPPTLANDTFR
TL
|
| Enzyme 20 Number of Residues |
602 |
| Enzyme 20 Molecular Weight |
66840.4 |
| Enzyme 20 Theoretical pI |
8.47 |
| Enzyme 20 GO Classification |
| Function |
|
| Process |
- cation transport
- establishment of localization
- ion transport
- monovalent inorganic cation transport
- sodium ion transport
- transmembrane transport
- transport
|
| Component |
|
|
| Enzyme 20 General Function |
Involved in transporter activity |
| Enzyme 20 Specific Function |
High-affinity sodium-dicarboxylate cotransporter that accepts a range of substrates with 4-5 carbon atoms. The stoichiometry is probably 3 Na(+) for 1 divalent succinate |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
- 17-37
56-76
83-103
139-159
230-250
279-299
337-357
373-393
462-482
506-526
547-567
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
8132324  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q8WWT9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
S13A3_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1809 bp
ATGGCGGCGCTGGCAGCAGCGGCCAAGAAGGTGTGGAGCGCGCGGCGGCTGCTGGTGCTG
CTGTTCACGCCGCTCGCGCTGCTGCCGGTGGTCTTCGCCCTCCCGCCCAAGGAAGGCCGC
TGCTTGTTTGTCATCCTGCTCATGGCGGTGTACTGGTGCACGGAGGCCCTGCCGCTCTCA
GTGACGGCGCTGCTGCCCATCGTCCTCTTCCCCTTCATGGGCATCTTGCCCTCCAACAAG
GTCTGCCCCCAGTACTTCCTCGACACCAACTTCCTCTTCCTCAGTGGGCTGATCATGGCC
AGCGCCATTGAGGAGTGGAACCTGCACCGGCGAATCGCCCTCAAGATCCTGATGCTTGTT
GGAGTCCAGCCGGCCAGGCTCATCCTGGGGATGATGGTGACCACCTCGTTCTTGTCCATG
TGGCTGAGCAACACCGCCTCCACTGCCATGATGCTTCCAATTGCCAATGCCATCCTGAAA
AGTCTCTTTGGCCAGAAGGAGGTTCGAAAGGACCCCAGCCAGGAGAGTGAAGAGAACACA
GCTGCTGTGCGGAGAAACGGCTACACACTGTGCCCACGGAGATGCAGTTTCTCGCCAAGC
ACAGAAGCCAAAGACCACCCTGGGGAGACAGAGGTTCCACTGGATCTGCCGGCTGACTCC
AGGAAGGAGGATGAATATCGTCGGAACATCTGGAAGGGCTTCCTCATCTCCATCCCCTAC
TCAGCCAGTATTGGGGGCACAGCCACACTCACGGGCACAGCCCCTAACCTCATCCTGCTT
GGCCAGCTCAAGAGTTTCTTTCCGCAGTGTGACGTGGTGAATTTCGGCTCCTGGTTCATT
TTCGCCTTCCCTCTTATGCTGTTGTTCCTGTTGGCAGGCTGGCTCTGGATCTCCTTCCTG
TACGGGGGACTGAGCTTCAGGGGCTGGAGGAAGAATAAATCTGAGATAAGAACCAATGCA
GAAGATAGGGCTCGAGCTGTAATTCGGGAAGAATACCAGAACCTGGGGCCCATCAAGTTT
GCCGAACAGGCTGTTTTCATCCTTTTCTGCATGTTTGCCATCCTCCTCTTCACCCGGGAC
CCGAAGTTCATCCCTGGCTGGGCCAGCCTCTTCAATCCTGGGTTTCTTTCTGATGCTGTC
ACCGGCGTGGCTATTGTCACCATCTTGTTCTTCTTCCCGTCCCAAAGGCCCTCTCTCAAG
TGGTGGTTTGACTTCAAAGCTCCCAACACAGAGACAGAGCCCTTGCTGACCTGGAAGAAG
GCCCAGGAGACAGTGCCCTGGAACATCATCCTTCTCCTGGGAGGGGGCTTCGCCATGGCC
AAAGGCTGTGAGGAATCGGGGCTGTCTGTATGGATTGGTGGGCAGCTGCACCCCCTGGAG
AATGTGCCCCCCGCCCTGGCTGTGCTGCTCATCACTGTGGTCATCGCCTTCTTCACTGAG
TTTGCCAGCAACACGGCGACCATCATCATCTTCCTGCCGGTCCTGGCAGAGCTGGCCATC
CGCCTGAGAGTGCACCCCCTGTATCTGATGATTCCGGGCACAGTCGGCTGCTCCTTTGCC
TTCATGCTCCCGGTCTCAACGCCCCCCAACTCCATCGCCTTCGCCTCTGGACACTTGCTG
GTCAAAGACATGGTGCGGACAGGCCTCCTGATGAACCTGATGGGTGTCCTGCTGCTCAGT
TTGGCTATGAATACCTGGGCACAGACCATCTTCCAGCTGGGCACCTTCCCGGACTGGGCT
GATATGTACTCGGTCAATGTCACAGCATTGCCACCCACCTTGGCCAATGACACATTTCGG
ACCCTCTGA
|
| Enzyme 20 GenBank Gene ID |
AF154121  |
| Enzyme 20 GeneCard ID |
SLC13A3  |
| Enzyme 20 GenAtlas ID |
SLC13A3  |
| Enzyme 20 HGNC ID |
HGNC:14430  |
| Enzyme 20 Chromosome Location |
2 |
| Enzyme 20 Locus |
20q12-q13.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Wang H, Fei YJ, Kekuda R, Yang-Feng TL, Devoe LD, Leibach FH, Prasad PD, Ganapathy V: Structure, function, and genomic organization of human Na(+)-dependent high-affinity dicarboxylate transporter. Am J Physiol Cell Physiol. 2000 May;278(5):C1019-30. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
8369 |
| Enzyme 21 Name |
17-beta-hydroxysteroid dehydrogenase type 6 |
| Enzyme 21 Synonyms |
- 17-beta-HSD 6
- 17-beta-HSD6
- 3-alpha->beta-hydroxysteroid epimerase
- 3-alpha->beta-HSE
- Oxidative 3-alpha hydroxysteroid dehydrogenase
|
| Enzyme 21 Gene Name |
HSD17B6 |
| Enzyme 21 Protein Sequence |
>17-beta-hydroxysteroid dehydrogenase type 6
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPIT
LCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSK
YGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQ
QYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTS
LADYILTRSWPKPAQAV
|
| Enzyme 21 Number of Residues |
317 |
| Enzyme 21 Molecular Weight |
35965.4 |
| Enzyme 21 Theoretical pI |
8.91 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in oxidoreductase activity |
| Enzyme 21 Specific Function |
NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3- alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha- androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
- retinol + NAD+ = retinal + NADH + H+ [RN:R02124]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
2338748  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
O14756  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
H17B6_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>954 bp
ATGTGGCTCTACCTGGCAGCCTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGGTGAGCCACCTCCAAGACAAGTATGTCTTTATCACGGGCTGTGACTCGGGC
TTTGGGAACCTACTGGCCAGACAGCTGGATGCACGAGGCTTGAGAGTGCTGGCTGCGTGT
CTGACGGAGAAGGGGGCCGAGCAGCTGAGGGGCCAGACGTCTGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGATGGAGAGCATCGCTGCAGCTACTCAGTGGGTGAAGGAGCAT
GTGGGGGACAGAGGACTCTGGGGACTGGTGAACAATGCAGGCATTCTTACACCAATTACC
TTATGTGAGTGGCTGAACACTGAGGACTCTATGAATATGCTCAAAGTGAACCTCATTGGT
GTGATCCAGGTGACCTTGAGCATGCTTCCTTTGGTGAGGAGAGCACGGGGAAGAATTGTC
AATGTCTCCAGCATTCTGGGAAGAGTTGCTTTCTTTGTAGGAGGCTACTGTGTCTCCAAG
TATGGAGTGGAAGCCTTTTCAGATATTCTGAGGCGTGAGATTCAACATTTTGGGGTGAAA
ATCAGCATAGTTGAACCTGGCTACTTCAGAACGGGAATGACAAACATGACACAGTCCTTA
GAGCGAATGAAGCAAAGTTGGAAAGAAGCCCCCAAGCATATTAAGGAGACCTATGGACAG
CAGTATTTTGATGCCCTTTACAATATCATGAAGGAAGGGCTGTTGAATTGTAGCACAAAC
CTGAACCTGGTCACTGACTGCATGGAACATGCTCTGACATCGGTGCATCCGCGAACTCGA
TATTCAGCTGGCTGGGATGCTAAATTTTTCTTCATCCCTCTATCTTATTTACCTACATCA
CTGGCAGACTACATTTTGACTAGATCTTGGCCCAAACCAGCCCAGGCAGTCTAA
|
| Enzyme 21 GenBank Gene ID |
AF016509  |
| Enzyme 21 GeneCard ID |
HSD17B6  |
| Enzyme 21 GenAtlas ID |
HSD17B6  |
| Enzyme 21 HGNC ID |
HGNC:23316  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
12q13 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Biswas MG, Russell DW: Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate. J Biol Chem. 1997 Jun 20;272(25):15959-66. [PubMed
]
- Huang XF, Luu-The V: Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase. J Biol Chem. 2000 Sep 22;275(38):29452-7. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Chetyrkin SV, Hu J, Gough WH, Dumaual N, Kedishvili NY: Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase. Arch Biochem Biophys. 2001 Feb 1;386(1):1-10. [PubMed
]
- Huang XF, Luu-The V: Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase. Biochim Biophys Acta. 2001 Aug 30;1520(2):124-30. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
8557 |
| Enzyme 22 Name |
Succinate-CoA ligase, ADP-forming, beta subunit |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
SUCLA2 |
| Enzyme 22 Protein Sequence |
>Succinate-CoA ligase, ADP-forming, beta subunit
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
|
| Enzyme 22 Number of Residues |
463 |
| Enzyme 22 Molecular Weight |
50318 |
| Enzyme 22 Theoretical pI |
7.50 |
| Enzyme 22 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Energy production and conversion |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
Not Available |
| Enzyme 22 Transmembrane Regions |
Not Available |
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
55957259  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q5T9Q4  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
Q5T9Q4_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1326 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGTATGGAA
TTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCAGATGAA
GCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAGGTTTTA
GCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAGATAGTT
TTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTGTTTACC
AAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGAAAATAT
CCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCTGTATTA
ATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCTGAAGCA
ATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTCCAGCTT
GCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATGGTCAAG
CTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATGGTGGAA
GATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAATTCAGCC
TATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGGGACAAA
GATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGCCTAGTA
AATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGGACTCCA
GCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCATTTAAG
CTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGAATCATG
CGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATTAAAATA
CCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATAGCGGAC
AGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTTGTAAAG
CTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAGTTGCCA
ATATGA
|
| Enzyme 22 GenBank Gene ID |
AL157369  |
| Enzyme 22 GeneCard ID |
SUCLA2  |
| Enzyme 22 GenAtlas ID |
SUCLA2  |
| Enzyme 22 HGNC ID |
HGNC:11448  |
| Enzyme 22 Chromosome Location |
13 |
| Enzyme 22 Locus |
13q12.2-q13.3 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
9242 |
| Enzyme 23 Name |
Trimethyllysine dioxygenase, mitochondrial |
| Enzyme 23 Synonyms |
- Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
- Epsilon-trimethyllysine hydroxylase
- TML hydroxylase
- TML-alpha-ketoglutarate dioxygenase
- TML dioxygenase
- TMLD
|
| Enzyme 23 Gene Name |
TMLHE |
| Enzyme 23 Protein Sequence |
>Trimethyllysine dioxygenase, mitochondrial
MWYHRLSHLHSRLQDLLKGGVIYPALPQPNFKSLLPLAVHWHHTASKSLTCAWQQHEDHF
ELKYANTVMRFDYVWLRDHCRSASCYNSKTHQRSLDTASVDLCIKPKTIRLDETTLFFTW
PDGHVTKYDLNWLVKNSYEGQKQKVIQPRILWNAEIYQQAQVPSVDCQSFLETNEGLKKF
LQNFLLYGIAFVENVPPTQEHTEKLAERISLIRETIYGRMWYFTSDFSRGDTAYTKLALD
RHTDTTYFQEPCGIQVFHCLKHEGTGGRTLLVDGFYAAEQVLQKAPEEFELLSKVPLKHE
YIEDVGECHNHMIGIGPVLNIYPWNKELYLIRYNNYDRAVINTVPYDVVHRWYTAHRTLT
IELRRPENEFWVKLKPGRVLFIDNWRVLHGRECFTGYRQLCGCYLTRDDVLNTARLLGLQ
A
|
| Enzyme 23 Number of Residues |
421 |
| Enzyme 23 Molecular Weight |
49517.2 |
| Enzyme 23 Theoretical pI |
7.79 |
| Enzyme 23 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- transition metal ion binding
- trimethyllysine dioxygenase activity
- vitamin binding
|
| Process |
- betaine metabolic process
- carnitine biosynthetic process
- carnitine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in oxidation reduction |
| Enzyme 23 Specific Function |
Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2 [RN:R03451]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9NVH6  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
TMLH_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1266 bp
ATGTGGTACCACAGATTGTCCCACCTACACAGCAGGCTTCAGGACTTGCTGAAGGGAGGA
GTCATATATCCGGCCCTTCCACAGCCCAACTTCAAAAGCTTACTTCCTTTAGCTGTCCAT
TGGCACCATACAGCCTCCAAGTCTCTGACTTGTGCTTGGCAGCAACATGAAGATCATTTT
GAGCTGAAATATGCTAATACCGTGATGCGCTTTGATTACGTCTGGCTTCGAGACCACTGC
CGCTCAGCATCGTGCTACAACTCTAAGACTCACCAGCGCAGCCTGGATACTGCCAGTGTG
GATTTATGTATCAAGCCAAAGACCATTCGTCTGGATGAGACCACACTCTTTTTCACTTGG
CCAGATGGTCATGTGACTAAATATGATTTGAATTGGCTGGTGAAAAACAGCTATGAAGGG
CAGAAACAAAAAGTCATCCAGCCTAGAATACTATGGAATGCTGAAATCTACCAGCAAGCC
CAAGTTCCATCGGTAGATTGCCAGAGCTTCTTAGAAACCAACGAGGGACTGAAGAAGTTT
CTGCAAAACTTTCTGCTCTATGGAATTGCATTCGTAGAAAATGTCCCTCCCACTCAAGAG
CACACAGAGAAGTTGGCAGAAAGGATCAGCTTAATCAGAGAAACCATTTATGGGAGGATG
TGGTATTTCACTTCAGACTTCTCCAGAGGTGACACTGCGTACACCAAGCTAGCTCTGGAT
CGGCACACTGACACTACCTATTTTCAAGAGCCCTGTGGCATTCAAGTGTTTCATTGTCTT
AAACATGAAGGAACTGGTGGCAGGACACTGCTAGTAGATGGATTCTATGCAGCAGAACAG
GTACTTCAAAAGGCACCTGAGGAATTTGAACTCCTCAGTAAAGTGCCATTGAAGCATGAA
TATATTGAAGATGTTGGAGAATGTCACAACCACATGATTGGGATTGGGCCAGTCTTAAAT
ATCTACCCATGGAATAAAGAGCTGTATTTGATCAGGTACAACAACTATGACCGGGCTGTC
ATCAATACCGTTCCTTATGATGTCGTCCATCGCTGGTATACAGCACACCGGACTCTAACG
ATAGAGTTGAGGAGACCTGAGAATGAGTTTTGGGTCAAACTAAAGCCTGGCAGGGTCCTA
TTTATAGACAACTGGCGTGTCCTACATGGCAGGGAATGCTTCACTGGCTACCGCCAACTG
TGTGGCTGCTATTTAACAAGAGATGATGTATTAAACACTGCTCGCCTCTTGGGGCTTCAG
GCTTAA
|
| Enzyme 23 GenBank Gene ID |
AF373407  |
| Enzyme 23 GeneCard ID |
TMLHE  |
| Enzyme 23 GenAtlas ID |
TMLHE  |
| Enzyme 23 HGNC ID |
HGNC:18308  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Vaz FM, Ofman R, Westinga K, Back JW, Wanders RJ: Molecular and Biochemical Characterization of Rat epsilon -N-Trimethyllysine Hydroxylase, the First Enzyme of Carnitine Biosynthesis. J Biol Chem. 2001 Sep 7;276(36):33512-7. Epub 2001 Jun 28. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Monfregola J, Cevenini A, Terracciano A, van Vlies N, Arbucci S, Wanders RJ, D'Urso M, Vaz FM, Ursini MV: Functional analysis of TMLH variants and definition of domains required for catalytic activity and mitochondrial targeting. J Cell Physiol. 2005 Sep;204(3):839-47. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
14401 |
| Enzyme 24 Name |
Prolyl 3-hydroxylase 1 |
| Enzyme 24 Synonyms |
- Growth suppressor 1
- Leucine- and proline-enriched proteoglycan 1
- Leprecan-1
|
| Enzyme 24 Gene Name |
LEPRE1 |
| Enzyme 24 Protein Sequence |
>Prolyl 3-hydroxylase 1
MAVRALKLLTTLLAVVAAASQAEVESEAGWGMVTPDLLFAEGTAAYARGDWPGVVLSMER
ALRSRAALRALRLRCRTQCAADFPWELDPDWSPSPAQASGAAALRDLSFFGGLLRRAACL
RRCLGPPAAHSLSEEMELEFRKRSPYNYLQVAYFKINKLEKAVAAAHTFFVGNPEHMEMQ
QNLDYYQTMSGVKEADFKDLETQPHMQEFRLGVRLYSEEQPQEAVPHLEAALQEYFVAYE
ECRALCEGPYDYDGYNYLEYNADLFQAITDHYIQVLNCKQNCVTELASHPSREKPFEDFL
PSHYNYLQFAYYNIGNYTQAVECAKTYLLFFPNDEVMNQNLAYYAAMLGEEHTRSIGPRE
SAKEYRQRSLLEKELLFFAYDVFGIPFVDPDSWTPEEVIPKRLQEKQKSERETAVRISQE
IGNLMKEIETLVEEKTKESLDVSRLTREGGPLLYEGISLTMNSKLLNGSQRVVMDGVISD
HECQELQRLTNVAATSGDGYRGQTSPHTPNEKFYGVTVFKALKLGQEGKVPLQSAHLYYN
VTEKVRRIMESYFRLDTPLYFSYSHLVCRTAIEEVQAERKDDSHPVHVDNCILNAETLVC
VKEPPAYTFRDYSAILYLNGDFDGGNFYFTELDAKTVTAEVQPQCGRAVGFSSGTENPHG
VKAVTRGQRCAIALWFTLDPRHSERDRVQADDLVKMLFSPEEMDLSQEQPLDAQQGPPEP
AQESLSGSESKPKDEL
|
| Enzyme 24 Number of Residues |
736 |
| Enzyme 24 Molecular Weight |
83393.2 |
| Enzyme 24 Theoretical pI |
4.79 |
| Enzyme 24 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in oxidoreductase activity |
| Enzyme 24 Specific Function |
Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro- Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
186928835  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q32P28  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
P3H1_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2211 bp
ATGGCGGTACGCGCGTTGAAGCTGCTGACCACACTGCTGGCTGTCGTGGCCGCTGCCTCC
CAAGCCGAGGTCGAGTCCGAGGCAGGATGGGGCATGGTGACGCCTGATCTGCTCTTCGCC
GAGGGGACCGCAGCCTACGCGCGCGGGGACTGGCCCGGGGTGGTCCTGAGCATGGAACGG
GCGCTGCGCTCCCGGGCAGCCCTCCGCGCCCTTCGCCTGCGCTGCCGCACCCAGTGTGCC
GCCGACTTCCCGTGGGAGCTGGACCCCGACTGGTCCCCCAGCCCGGCCCAGGCCTCGGGC
GCCGCCGCCCTGCGCGACCTGAGCTTCTTCGGGGGCCTTCTGCGTCGCGCTGCCTGCCTG
CGCCGCTGCCTCGGGCCGCCGGCCGCCCACTCGCTCAGCGAAGAGATGGAGCTGGAGTTC
CGCAAGCGGAGCCCCTACAACTACCTGCAGGTCGCCTACTTCAAGATCAACAAGTTGGAG
AAAGCTGTTGCTGCAGCACACACCTTCTTCGTGGGCAATCCTGAGCACATGGAAATGCAG
CAGAACCTAGACTATTACCAAACCATGTCTGGAGTGAAGGAGGCCGACTTCAAGGATCTT
GAGACTCAACCCCATATGCAAGAATTTCGACTGGGAGTGCGACTCTACTCAGAGGAACAG
CCACAGGAAGCTGTGCCCCACCTAGAGGCGGCGCTGCAAGAATACTTTGTGGCCTATGAG
GAGTGCCGTGCCCTCTGCGAAGGGCCCTATGACTACGATGGCTACAACTACCTTGAGTAC
AACGCTGACCTCTTCCAGGCCATCACAGATCATTACATCCAGGTCCTCAACTGTAAGCAG
AACTGTGTCACGGAGCTTGCTTCCCACCCAAGTCGAGAGAAGCCCTTTGAAGACTTCCTC
CCATCGCATTATAATTATCTGCAGTTTGCCTACTATAACATTGGGAATTATACACAGGCT
GTTGAATGTGCCAAGACCTATCTTCTCTTCTTCCCCAATGACGAGGTGATGAACCAAAAT
TTGGCCTATTATGCAGCTATGCTTGGAGAAGAACACACCAGATCCATCGGCCCCCGTGAG
AGTGCCAAGGAGTACCGACAGCGAAGCCTACTGGAAAAAGAACTGCTTTTCTTCGCTTAT
GATGTTTTTGGAATTCCCTTTGTGGATCCGGATTCATGGACTCCAGAAGAAGTGATTCCC
AAGAGATTGCAAGAGAAACAGAAGTCAGAACGGGAAACAGCCGTACGCATCTCCCAGGAG
ATTGGGAACCTTATGAAGGAAATCGAGACCCTTGTGGAAGAGAAGACCAAGGAGTCACTG
GATGTGAGCAGACTGACCCGGGAAGGTGGCCCCCTGCTGTATGAAGGCATCAGTCTCACC
ATGAACTCCAAACTCCTGAATGGTTCCCAGCGGGTGGTGATGGACGGCGTAATCTCTGAC
CACGAGTGTCAGGAGCTGCAGAGACTGACCAATGTGGCAGCAACCTCAGGAGATGGCTAC
CGGGGTCAGACCTCCCCACATACTCCCAATGAAAAGTTCTATGGTGTCACTGTCTTCAAA
GCCCTCAAGCTGGGGCAAGAAGGCAAAGTTCCTCTGCAGAGTGCCCACCTGTACTACAAC
GTGACGGAGAAGGTGCGGCGCATCATGGAGTCCTACTTCCGCCTGGATACGCCCCTCTAC
TTTTCCTACTCTCATCTGGTGTGCCGCACTGCCATCGAAGAGGTCCAGGCAGAGAGGAAG
GATGATAGTCATCCAGTCCACGTGGACAACTGCATCCTGAATGCCGAGACCCTCGTGTGT
GTCAAAGAGCCCCCAGCCTACACCTTCCGCGACTACAGCGCCATCCTTTACCTAAATGGG
GACTTCGATGGCGGAAACTTTTATTTCACTGAACTGGATGCCAAGACCGTGACGGCAGAG
GTGCAGCCTCAGTGTGGAAGAGCCGTGGGATTCTCTTCAGGCACTGAAAACCCACATGGA
GTGAAGGCTGTCACCAGGGGGCAGCGCTGTGCCATCGCCCTGTGGTTCACCCTGGACCCT
CGACACAGCGAGCGGGACAGGGTGCAGGCAGATGACCTGGTGAAGATGCTCTTCAGCCCA
GAAGAGATGGACCTCTCCCAGGAGCAGCCCCTGGATGCCCAGCAGGGCCCCCCCGAACCT
GCACAAGAGTCTCTCTCAGGCAGTGAATCGAAGCCCAAGGATGAGCTATGA
|
| Enzyme 24 GenBank Gene ID |
NM_022356.3  |
| Enzyme 24 GeneCard ID |
LEPRE1  |
| Enzyme 24 GenAtlas ID |
LEPRE1  |
| Enzyme 24 HGNC ID |
HGNC:19316  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
1p34.1 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Kaul SC, Sugihara T, Yoshida A, Nomura H, Wadhwa R: Gros1, a potential growth suppressor on chromosome 1: its identity to basement membrane-associated proteoglycan, leprecan. Oncogene. 2000 Jul 27;19(32):3576-83. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, Leikin S, Makareeva E, Kuznetsova NV, Rosenbaum KN, Tifft CJ, Bulas DI, Kozma C, Smith PA, Eyre DR, Marini JC: Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet. 2007 Mar;39(3):359-65. Epub 2007 Feb 4. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
14402 |
| Enzyme 25 Name |
Prolyl 3-hydroxylase 2 |
| Enzyme 25 Synonyms |
- Leprecan-like protein 1
- Myxoid liposarcoma-associated protein 4
|
| Enzyme 25 Gene Name |
LEPREL1 |
| Enzyme 25 Protein Sequence |
>Prolyl 3-hydroxylase 2
MRERIWAPPLLLLLPLLLPPPLWGGPPDSPRRELELEPGPLQPFDLLYASGAAAYYSGDY
ERAVRDLEAALRSHRRLREIRTRCARHCAARHPLPPPPPGEGPGAELPLFRSLLGRARCY
RSCETQRLGGPASRHRVSEDVRSDFQRRVPYNYLQRAYIKLNQLEKAVEAAHTFFVANPE
HMEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREY
FVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSP
IENFLPLHYDYLQFAYYRVGEYVKALECAKAYLLCHPDDEDVLDNVDYYESLLDDSIDPA
SIEAREDLTMFVKRHKLESELIKSAAEGLGFSYTEPNYWIRYGGRQDENRVPSGVNVEGA
EVHGFSMGKKLSPKIDRDLREGGPLLYENITFVYNSEQLNGTQRVLLDNVLSEEQCRELH
SVASGIMLVGDGYRGKTSPHTPNEKFEGATVLKALKSGYEGRVPLKSARLFYDISEKARR
IVESYFMLNSTLYFSYTHMVCRTALSGQQDRRNDLSHPIHADNCLLDPEANECWKEPPAY
TFRDYSALLYMNDDFEGGEFIFTEMDAKTVTASIKPKCGRMISFSSGGENPHGVKAVTKG
KRCAVALWFTLDPLYRELERIQADEVIAILDQEQQGKHELNINPKDEL
|
| Enzyme 25 Number of Residues |
708 |
| Enzyme 25 Molecular Weight |
80983.7 |
| Enzyme 25 Theoretical pI |
5.47 |
| Enzyme 25 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in oxidoreductase activity |
| Enzyme 25 Specific Function |
Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
27526730  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q8IVL5  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
P3H2_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>2127 bp
ATGCGGGAGCGCATCTGGGCGCCGCCGCTGCTGCTGCTGCTGCCGCTGCTACTGCCGCCG
CCACTGTGGGGCGGCCCCCCGGACAGCCCACGCCGGGAGCTGGAGCTGGAGCCCGGGCCT
CTGCAGCCCTTCGACCTGCTCTACGCCAGCGGCGCGGCCGCCTACTACAGCGGAGACTAC
GAGCGAGCGGTGCGCGACTTGGAAGCGGCGCTGCGCAGCCACCGGCGCCTGCGGGAAATC
CGCACGCGCTGTGCCCGCCACTGCGCGGCGCGCCACCCGCTCCCGCCCCCGCCCCCCGGC
GAGGGCCCCGGCGCTGAGCTGCCCCTTTTCCGCTCCTTGTTGGGGCGGGCGCGCTGTTAT
CGCAGCTGTGAGACCCAGCGCCTCGGGGGCCCCGCATCCCGCCACCGCGTCAGCGAGGAT
GTGCGCAGCGACTTCCAGCGCAGAGTGCCCTACAACTACCTGCAGCGGGCCTACATCAAG
CTTAACCAGCTCGAAAAAGCAGTGGAAGCAGCTCACACATTTTTCGTGGCTAACCCTGAG
CACATGGAAATGCAGCAGAACATTGAGAATTACAGGGCGACAGCTGGTGTTGAAGCATTG
CAGTTGGTAGACAGAGAAGCCAAGCCACACATGGAGAGTTACAATGCAGGAGTTAAACAT
TATGAGGCTGATGACTTTGAGATGGCTATCAGGCATTTCGAACAAGCCTTAAGAGAATAT
TTCGTTGAAGATACAGAATGCCGGACCCTATGTGAGGGGCCTCAGAGATTTGAAGAATAT
GAGTATTTAGGGTATAAGGCTGGTCTGTATGAAGCTATTGCAGATCACTACATGCAGGTG
CTTGTTTGTCAGCATGAATGTGTGAGGGAACTTGCCACCCGCCCTGGCCGCCTCTCTCCC
ATCGAGAATTTTCTTCCTCTGCACTATGATTACCTACAGTTTGCCTACTATCGAGTTGGT
GAGTATGTGAAAGCCCTGGAGTGTGCCAAAGCCTATCTTCTATGCCATCCAGATGATGAG
GATGTCCTAGACAATGTGGATTACTATGAGAGTCTGCTGGATGATAGCATTGACCCGGCA
TCCATTGAGGCCAGAGAGGATTTAACAATGTTTGTGAAACGTCATAAGCTGGAGTCTGAG
CTGATAAAATCAGCTGCAGAAGGTCTGGGGTTTTCATACACTGAACCGAATTATTGGATC
AGATATGGAGGACGACAGGATGAGAATCGGGTCCCTTCAGGAGTGAACGTAGAGGGAGCA
GAAGTTCATGGATTCTCAATGGGAAAAAAGCTATCACCCAAGATAGATCGAGACCTAAGA
GAAGGTGGTCCTCTACTCTATGAGAACATCACATTCGTCTACAACTCGGAGCAGCTGAAC
GGGACTCAGCGGGTTCTCCTGGATAACGTCCTGTCGGAAGAACAGTGCCGGGAGCTCCAC
AGCGTGGCCAGTGGAATCATGCTTGTTGGTGATGGATACAGAGGAAAAACTTCACCCCAT
ACACCCAATGAAAAGTTTGAAGGTGCAACTGTCCTGAAAGCACTCAAATCTGGTTATGAA
GGTCGAGTCCCACTGAAGAGCGCTCGTCTGTTTTATGACATCAGCGAAAAGGCTCGAAGG
ATTGTAGAATCTTATTTTATGCTGAACTCAACTCTGTATTTTTCCTATACACACATGGTC
TGCCGAACAGCCCTGTCTGGTCAGCAGGATAGAAGAAATGACCTCAGTCATCCCATCCAT
GCTGACAACTGTTTGTTGGATCCAGAGGCCAACGAATGCTGGAAGGAGCCTCCTGCTTAC
ACATTTCGAGACTATAGTGCTCTCCTATATATGAATGATGACTTTGAAGGAGGAGAATTC
ATATTCACAGAGATGGATGCTAAGACTGTGACTGCCTCTATAAAACCAAAATGTGGGCGC
ATGATCAGCTTCTCATCTGGAGGAGAGAACCCTCATGGGGTGAAGGCAGTCACCAAGGGA
AAGAGGTGTGCTGTGGCTCTGTGGTTCACCTTGGACCCACTTTATAGAGAATTGGAGCGA
ATACAGGCTGATGAAGTGATTGCAATTCTGGATCAAGAACAGCAAGGGAAGCATGAACTG
AATATCAACCCTAAAGATGAGCTATAA
|
| Enzyme 25 GenBank Gene ID |
AJ430351  |
| Enzyme 25 GeneCard ID |
LEPREL1  |
| Enzyme 25 GenAtlas ID |
LEPREL1  |
| Enzyme 25 HGNC ID |
HGNC:19317  |
| Enzyme 25 Chromosome Location |
3 |
| Enzyme 25 Locus |
3q28 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Thelin-Jarnum S, Lassen C, Panagopoulos I, Mandahl N, Aman P: Identification of genes differentially expressed in TLS-CHOP carrying myxoid liposarcomas. Int J Cancer. 1999 Sep 24;83(1):30-3. [PubMed
]
- Jarnum S, Kjellman C, Darabi A, Nilsson I, Edvardsen K, Aman P: LEPREL1, a novel ER and Golgi resident member of the Leprecan family. Biochem Biophys Res Commun. 2004 Apr 30;317(2):342-51. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
14403 |
| Enzyme 26 Name |
Prolyl 3-hydroxylase 3 |
| Enzyme 26 Synonyms |
- Leprecan-like protein 2
- Protein B
|
| Enzyme 26 Gene Name |
LEPREL2 |
| Enzyme 26 Protein Sequence |
>Prolyl 3-hydroxylase 3
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALL
REALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALR
RADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTF
FVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLE
EALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGE
TATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQ
AQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREK
LREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGV
LLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSE
RVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWRE
PPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWA
VTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQ
RVQDKTGRAPRVREEL
|
| Enzyme 26 Number of Residues |
736 |
| Enzyme 26 Molecular Weight |
81835.7 |
| Enzyme 26 Theoretical pI |
6.26 |
| Enzyme 26 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in iron ion binding |
| Enzyme 26 Specific Function |
Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2 [RN:R03218]
|
| Enzyme 26 Pfam Domain Function |
Not Available |
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
27526728  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q8IVL6  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
P3H3_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>2211 bp
ATGCTCCGGCTCCTCCGGCCGCTGCTGCTACTGCTGCTGCTGCCTCCCCCGGGGTCCCCT
GAGCCCCCCGGCCTGACCCAGCTGTCCCCGGGGGCGCCCCCGCAGGCCCCCGACTTGCTC
TACGCTGACGGGCTGCGCGCCTACGCGGCCGGGGCTTGGGCGCCGGCCGTGGCGCTGCTG
CGGGAGGCGCTGCGGAGCCAGGCGGCGCTGGGCCGGGTGCGGCTGGATTGCGGGGCGAGC
TGCGCGGCCGATCCGGGCGCCGCGCTCCCCGCCGTGCTTCTCGGGGCCCCGGAGCCCGAC
TCCGGGCCGGGACCCACGCAGGGGTCCTGGGAGCGACAGCTTCTCCGTGCAGCGCTCCGC
CGCGCAGACTGCCTGACCCAGTGCGCAGCACGGAGGCTGGGCCCCGGGGGCGCGGCGCGG
CTTCGCGTGGGGAGCGCGCTCCGGGACGCCTTCCGCCGTCGGGAGCCCTACAACTACCTG
CAGAGGGCCTATTACCAGTTGAAGAAGCTGGATCTGGCAGCTGCGGCAGCACACACCTTC
TTTGTAGCAAACCCCATGCACCTGCAGATGCGGGAGGACATGGCTAAGTACAGACGAATG
TCGGGAGTTCGGCCCCAGAGCTTCCGGGACCTGGAGACGCCCCCACACTGGGCAGCCTAT
GACACTGGCCTGGAGCTACTGGGGCGCCAGGAGGCAGGACTGGCACTGCCCAGGCTAGAG
GAGGCTCTTCAGGGGAGCCTGGCCCAGATGGAGAGCTGCCGTGCTGACTGTGAGGGGCCT
GAGGAGCAGCAGGGGGCTGAAGAAGAGGAGGATGGGGCTGCGAGCCAGGGGGGCCTCTAT
GAGGCCATTGCAGGACACTGGATTCAGGTCCTGCAGTGCCGGCAACGCTGTGTGGGGGAA
ACAGCCACACGCCCTGGTCGCAGCTTCCCTGTCCCAGACTTCCTTCCCAACCAGCTGAGG
CGGCTACATGAGGCCCATGCTCAGGTGGGCAATCTGTCCCAGGCTATAGAAAATGTCCTG
AGTGTCCTGCTCTTCTACCCGGAGGATGAGGCTGCCAAGAGGGCTCTGAACCAGTACCAG
GCCCAGCTGGGAGAGCCGAGACCTGGCCTCGGACCCAGAGAGGACATCCAGCGCTTCATC
CTCCGATCCCTGGGGGAGAAGAGGCAGCTCTACTATGCCATGGAGCACCTGGGGACCAGC
TTCAAGGATCCTGACCCCTGGACCCCTGCAGCTCTCATCCCTGAGGCACTTAGAGAAAAG
CTCAGAGAGGATCAAGAGAAGAGGCCTTGGGACCATGAGCCCGTGAAGCCAAAGCCCTTG
ACCTACTGGAAGGATGTCCTTCTCCTGGAGGGTGTGACCTTGACCCAGGATTCCAGGCAG
CTGAATGGGTCGGAGCGGGCGGTGTTGGATGGGCTGCTCACCCCAGCCGAGTGTGGGGTG
CTGCTGCAGCTGGCTAAGGATGCAGCTGGGGCTGGAGCCAGGTCTGGCTATCGTGGTCGC
CGCTCCCCTCACACCCCCCATGAACGCTTCGAGGGGCTCACGGTGCTTAAGGCTGCGCAG
CTGGCCCGGGCTGGGACAGTGGGCAGTCAGGGTGCTAAGCTGCTTCTGGAGGTGAGCGAG
CGGGTGCGGACCTTGACCCAGGCCTACTTCTCCCCGGAACGGCCCCTGCATCTGTCCTTC
ACCCACCTGGTGTGCCGCAGCGCCATAGAAGGAGAGCAAGAGCAGCGCATGGACCTGAGT
CACCCAGTGCACGCAGACAACTGCGTCCTGGACCCTGACACGGGAGAGTGCTGGCGGGAG
CCCCCAGCCTACACCTATCGGGACTACAGCGGACTCCTCTACCTCAACGATGACTTCCAG
GGTGGGGACCTGTTCTTCACGGAGCCCAACGCCCTCACTGTCACGGCTCGGGTGCGTCCT
CGCTGTGGGCGCCTTGTGGCCTTCAGCTCCGGTGTCGAGAATCCCCATGGGGTGTGGGCC
GTGACTCGGGGACGGCGCTGTGCCCTGGCACTGTGGCACACGTGGGCACCTGAGCACAGG
GAGCAGGAGTGGATAGAAGCCAAAGAACTGCTGCAGGAGTCACAGGAGGAGGAGGAAGAG
GAAGAGGAAGAAATGCCCAGCAAAGACCCTTCCCCAGAGCCCCCTAGCCGCAGGCACCAG
AGGGTCCAAGACAAGACTGGAAGGGCACCTCGGGTTCGGGAGGAGCTGTGA
|
| Enzyme 26 GenBank Gene ID |
AJ430349  |
| Enzyme 26 GeneCard ID |
LEPREL2  |
| Enzyme 26 GenAtlas ID |
LEPREL2  |
| Enzyme 26 HGNC ID |
HGNC:19318  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
12q13 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed
]
- Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed
]
- Jarnum S, Kjellman C, Darabi A, Nilsson I, Edvardsen K, Aman P: LEPREL1, a novel ER and Golgi resident member of the Leprecan family. Biochem Biophys Res Commun. 2004 Apr 30;317(2):342-51. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
14855 |
| Enzyme 27 Name |
Prolyl 4-hydroxylase subunit alpha-3 |
| Enzyme 27 Synonyms |
- 4-PH alpha-3
- Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-3
|
| Enzyme 27 Gene Name |
P4HA3 |
| Enzyme 27 Protein Sequence |
>Prolyl 4-hydroxylase subunit alpha-3
MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEA
RLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGY
EKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLT
GDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRA
GNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDT
YEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEA
QKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRP
PYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIY
ANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSS
SPED
|
| Enzyme 27 Number of Residues |
544 |
| Enzyme 27 Molecular Weight |
61125.7 |
| Enzyme 27 Theoretical pI |
6.46 |
| Enzyme 27 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
- peptidyl-proline dioxygenase activity
- procollagen-proline 4-dioxygenase activity
- procollagen-proline dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 27 General Function |
Involved in oxidoreductase activity |
| Enzyme 27 Specific Function |
Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins |
| Enzyme 27 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 27 Reactions |
- procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2 [RN:R03219]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
36962719  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q7Z4N8  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
P4HA3_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1635 bp
ATGGGTCCTGGGGCGCGGCTGGCGGCGCTGCTGGCGGTGCTGGCGCTCGGGACAGGAGAC
CCAGAAAGGGCTGCGGCTCGGGGCGACACGTTCTCGGCGCTGACCAGCGTGGCGCGCGCC
CTGGCGCCCGAGCGCCGGCTGCTGGGGCTGCTGAGGCGGTACCTGCGCGGGGAGGAGGCG
CGGCTGCGGGACCTGACTAGATTCTACGACAAGGTACTTTCTTTGCATGAGGATTCAACA
ACCCCTGTGGCTAACCCTCTGCTTGCATTTACTCTCATCAAACGCCTGCAGTCTGACTGG
AGGAATGTGGTACATAGTCTGGAGGCCAGTGAGAACATCCGAGCTCTGAAGGATGGCTAT
GAGAAGGTGGAGCAAGACCTTCCAGCCTTTGAGGACCTTGAGGGAGCAGCAAGGGCCCTG
ATGCGGCTGCAGGACGTGTACATGCTCAATGTGAAAGGCCTGGCCCGAGGTGTCTTTCAG
AGAGTCACTGGCTCTGCCATCACTGACCTGTACAGCCCCAAACGGCTCTTTTCTCTCACA
GGGGATGACTGCTTCCAAGTTGGCAAGGTGGCCTATGACATGGGGGATTATTACCATGCC
ATTCCATGGCTGGAGGAGGCTGTCAGTCTCTTCCGAGGATCTTACGGAGAGTGGAAGACA
GAGGATGAGGCAAGTCTAGAAGATGCCTTGGATCACTTGGCCTTTGCTTATTTCCGGGCA
GGAAATGTTTCGTGTGCCCTCAGCCTCTCTCGGGAGTTTCTTCTCTACAGCCCAGATAAT
AAGAGGATGGCCAGGAATGTCTTGAAATATGAAAGGCTCTTGGCAGAGAGCCCCAACCAC
GTGGTAGCTGAGGCTGTCATCCAGAGGCCCAATATACCCCACCTGCAGACCAGAGACACC
TACGAGGGGCTATGTCAGACCCTGGGTTCCCAGCCCACTCTCTACCAGATCCCTAGCCTC
TACTGTTCCTATGAGACCAATTCCAACGCCTACCTGCTGCTCCAGCCCATCCGGAAGGAG
GTCATCCACCTGGAGCCCTACATTGCTCTCTACCATGACTTCGTCAGTGACTCAGAGGCT
CAGAAAATTAGAGAACTTGCAGAACCATGGCTACAGAGGTCAGTGGTGGCATCAGGGGAG
AAGCAGTTACAAGTGGAGTACCGCATCAGCAAAAGTGCCTGGCTGAAGGACACTGTTGAC
CCAAAACTGGTGACCCTCAACCACCGCATTGCTGCCCTCACAGGCCTTGATGTCCGGCCT
CCCTATGCAGAGTATCTGCAGGTGGTGAACTATGGCATCGGAGGACACTATGAGCCTCAC
TTTGACCATGCTACGTCACCAAGCAGCCCCCTCTACAGAATGAAGTCAGGAAACCGAGTT
GCAACATTTATGATCTATCTGAGCTCGGTGGAAGCTGGAGGAGCCACAGCCTTCATCTAT
GCCAACCTCAGCGTGCCTGTGGTTAGGAATGCAGCACTGTTTTGGTGGAACCTGCACAGG
AGTGGTGAAGGGGACAGTGACACACTTCATGCTGGCTGTCCTGTCCTGGTGGGAGATAAG
TGGGTGGCCAACAAGTGGATACATGAGTATGGACAGGAATTCCGCAGACCCTGCAGCTCC
AGCCCTGAAGACTGA
|
| Enzyme 27 GenBank Gene ID |
AY313448  |
| Enzyme 27 GeneCard ID |
P4HA3  |
| Enzyme 27 GenAtlas ID |
P4HA3  |
| Enzyme 27 HGNC ID |
HGNC:30135  |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
11q13.4 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Kukkola L, Hieta R, Kivirikko KI, Myllyharju J: Identification and characterization of a third human, rat, and mouse collagen prolyl 4-hydroxylase isoenzyme. J Biol Chem. 2003 Nov 28;278(48):47685-93. Epub 2003 Sep 18. [PubMed
]
- Van Den Diepstraten C, Papay K, Bolender Z, Brown A, Pickering JG: Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque. Circulation. 2003 Aug 5;108(5):508-11. Epub 2003 Jul 21. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
15216 |
| Enzyme 28 Name |
Succinate dehydrogenase complex, subunit C delta5 alternative splicing variant |
| Enzyme 28 Synonyms |
- SubName: cDNA FLJ57876, highly similar to Homo sapiens succinate dehydrogenase complex, subunit C, transcript variant 2, mRNA
|
| Enzyme 28 Gene Name |
SDHC |
| Enzyme 28 Protein Sequence |
>Succinate dehydrogenase complex, subunit C delta5 alternative splicing variant
MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYS
WSLPMAMSICHRGTGIALSADVGPRKRPEDSPAIPVWSGCPGSYCVVLYGAGSHVKKGGS
QHHLPTHYYIHPSFCLSFLSPAWEKFSLFV
|
| Enzyme 28 Number of Residues |
150 |
| Enzyme 28 Molecular Weight |
16650.2 |
| Enzyme 28 Theoretical pI |
9.59 |
| Enzyme 28 GO Classification |
| Function |
- catalytic activity
- electron carrier activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- succinate dehydrogenase activity
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- tricarboxylic acid cycle
|
| Component |
|
|
| Enzyme 28 General Function |
Involved in succinate dehydrogenase activity |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
78096641  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q3C2D8  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
Q3C2D8_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>453 bp
ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATGCTGTTCCTTTGGGAACCACGGCCAAAGAAGAGATGGAGCGG
TTCTGGAATAAGAATATAGGTTCAAACCGTCCTCTGTCTCCCCACATTACTATCTACAGT
TGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACTGGTATTGCTTTGAGTGCA
GATGTGGGACCTAGGAAAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTTGT
CCTGGTTCTTACTGTGTTGTCCTCTATGGGGCTGGCAGCCATGTGAAGAAAGGAGGCTCC
CAGCATCATCTTCCTACACATTATTACATTCACCCATCTTTCTGTTTGTCATTCTTATCT
CCAGCCTGGGAAAAGTTCTCCTTATTTGTTTAG
|
| Enzyme 28 GenBank Gene ID |
AB211235  |
| Enzyme 28 GeneCard ID |
SDHC  |
| Enzyme 28 GenAtlas ID |
SDHC  |
| Enzyme 28 HGNC ID |
HGNC:10682  |
| Enzyme 28 Chromosome Location |
1 |
| Enzyme 28 Locus |
1q23.3 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
15217 |
| Enzyme 29 Name |
Integral membrane protein CII-3b |
| Enzyme 29 Synonyms |
- SubName: Succinate dehydrogenase complex, subunit C delta3 alternative splicing variant
- SubName: Succinate dehydrogenase complex, subunit C, integral membrane protein, 15kDa, isoform CRA_g
|
| Enzyme 29 Gene Name |
SDHC |
| Enzyme 29 Protein Sequence |
>Integral membrane protein CII-3b
MAALLLRHVGRHCLRAHFSPQLCIRNWSLPMAMSICHRGTGIALSAGVSLFGMSALLLPG
NFESYLELVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVV
VLVLTVLSSMGLAAM
|
| Enzyme 29 Number of Residues |
135 |
| Enzyme 29 Molecular Weight |
14769.7 |
| Enzyme 29 Theoretical pI |
10.08 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- electron carrier activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- succinate dehydrogenase activity
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- tricarboxylic acid cycle
|
| Component |
- cell part
- membrane
- membrane part
- plasma membrane part
- plasma membrane succinate dehydrogenase complex
|
|
| Enzyme 29 General Function |
Involved in succinate dehydrogenase activity |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
78096639  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
O75609  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
O75609_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>408 bp
ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATTGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACT
GGTATTGCTTTGAGTGCAGGGGTCTCTCTTTTTGGCATGTCGGCCCTGTTACTCCCTGGG
AACTTTGAGTCTTATTTGGAACTTGTGAAGTCCCTGTGTCTGGGGCCAGCACTGATCCAC
ACAGCTAAGTTTGCACTTGTCTTCCCTCTCATGTATCATACCTGGAATGGGATCCGACAC
TTGATGTGGGACCTAGGAAAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTT
GTCCTGGTTCTTACTGTGTTGTCCTCTATGGGGCTGGCAGCCATGTGA
|
| Enzyme 29 GenBank Gene ID |
AB211234  |
| Enzyme 29 GeneCard ID |
SDHC  |
| Enzyme 29 GenAtlas ID |
SDHC  |
| Enzyme 29 HGNC ID |
HGNC:10682  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
1q23.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Wohllk N, Thomas PM, Huang E, Cote GJ: A human succinate-ubiquinone oxidoreductase CII-3 subunit gene ending in a polymorphic dinucleotide repeat is located within the sulfonylurea receptor (SUR) gene. Mol Genet Metab. 1998 Nov;65(3):187-90. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
15235 |
| Enzyme 30 Name |
Putative uncharacterized protein PHYH |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
PHYH |
| Enzyme 30 Protein Sequence |
>Putative uncharacterized protein PHYH
MRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLIN
KPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPH
DYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISC
HFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
|
| Enzyme 30 Number of Residues |
238 |
| Enzyme 30 Molecular Weight |
27291.2 |
| Enzyme 30 Theoretical pI |
8.38 |
| Enzyme 30 GO Classification |
Not Available |
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
83281447  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
A8MTS8  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
A8MTS8_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>717 bp
ATGAGAGATGTGACCATTTCGAAATCCGAATATGCTCCAAGTGAGAAGATGATCACGAAG
GTCCAGGATTTCCAGGAAGATAAGGAGCTCTTCAGATACTGCACTCTCCCCGAGATTCTG
AAATATGTGGAGTGCTTCACTGGACCTAATATTATGGCCATGCACACAATGTTGATAAAC
AAACCTCCAGATTCTGGCAAGAAGACGTCCCGTCACCCCCTGCACCAGGACCTGCACTAT
TTCCCCTTCAGGCCCAGCGATCTCATCGTTTGCGCCTGGACGGCGATGGAGCACATCAGC
CGGAACAACGGCTGTCTGGTTGTGCTCCCAGGCACACACAAGGGCTCCCTGAAGCCCCAC
GATTACCCCAAGTGGGAGGGGGGAGTTAACAAAATGTTCCACGGGATCCAGGACTACGAG
GAAAACAAGGCCCGGGTGCACCTGGTGATGGAGAAGGGCGACACTGTTTTCTTCCATCCT
TTGCTCATCCACGGATCTGGTCAGAATAAAACCCAGGGATTCCGGAAGGCAATTTCCTGC
CATTTCGCCAGTGCCGATTGCCACTACATTGACGTGAAGGGCACCAGTCAAGAAAACATC
GAGAAGGAAGTTGTAGGAATAGCACATAAATTCTTTGGAGCTGAAAATAGCGTGAACTTG
AAGGATATTTGGATGTTTCGAGCTCGACTTGTGAAAGGAGAAAGAACCAATCTTTGA
|
| Enzyme 30 GenBank Gene ID |
NM_001037537.1  |
| Enzyme 30 GeneCard ID |
PHYH  |
| Enzyme 30 GenAtlas ID |
PHYH  |
| Enzyme 30 HGNC ID |
HGNC:8940  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
10p13 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
16431 |
| Enzyme 31 Name |
Putative uncharacterized protein |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
BBOX1 |
| Enzyme 31 Protein Sequence |
>Putative uncharacterized protein
MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDV
NIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSEL
QLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHT
WQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQK
LKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIF
DVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISR
HLEGAYADWDVVMSRLRILRQRVENGN
|
| Enzyme 31 Number of Residues |
387 |
| Enzyme 31 Molecular Weight |
44715 |
| Enzyme 31 Theoretical pI |
6.73 |
| Enzyme 31 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
Not Available |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
B2R8L7  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
B2R8L7_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
Not Available |
| Enzyme 31 GenBank Gene ID |
AK313422  |
| Enzyme 31 GeneCard ID |
B2R8L7  |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
Not Available |
| Enzyme 31 Chromosome Location |
11 |
| Enzyme 31 Locus |
11p14.2 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
16432 |
| Enzyme 32 Name |
cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3) |
| Enzyme 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
PLOD3 |
| Enzyme 32 Protein Sequence |
>cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3)
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
|
| Enzyme 32 Number of Residues |
738 |
| Enzyme 32 Molecular Weight |
84786 |
| Enzyme 32 Theoretical pI |
5.95 |
| Enzyme 32 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- procollagen-lysine 5-dioxygenase activity
|
| Process |
- macromolecule metabolism
- metabolism
- physiological process
- protein metabolism
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bound organelle
- membrane-bound organelle
- organelle
|
|
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
B2R6W6  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
B2R6W6_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
Not Available |
| Enzyme 32 GenBank Gene ID |
AK312743  |
| Enzyme 32 GeneCard ID |
B2R6W6  |
| Enzyme 32 GenAtlas ID |
Not Available |
| Enzyme 32 HGNC ID |
Not Available |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
16498 |
| Enzyme 33 Name |
cDNA, FLJ92337, highly similar to Homo sapiens succinate dehydrogenase complex, subunit B, iron sulfur (Ip) (SDHB), mRNA (Succinate dehydrogenase complex, subunit B, iron sulfur (Ip), isoform CRA_a) |
| Enzyme 33 Synonyms |
Not Available |
| Enzyme 33 Gene Name |
SDHB |
| Enzyme 33 Protein Sequence |
>cDNA, FLJ92337, highly similar to Homo sapiens succinate dehydrogenase complex, subunit B, iron sulfur (Ip) (SDHB), mRNA (Succinate dehydrogenase complex, subunit B, iron sulfur (Ip), isoform CRA_a)
MAAVVALSLRRRLPATTLGGACLQASRGAQTAAATAPRIKKFAIYRWDPDKAGDKPHMQT
YEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN
LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKL
DGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSL
YRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKASV
|
| Enzyme 33 Number of Residues |
280 |
| Enzyme 33 Molecular Weight |
31630 |
| Enzyme 33 Theoretical pI |
8.92 |
| Enzyme 33 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- electron transporter activity
- ion binding
- iron ion binding
- oxidoreductase activity
- transition metal ion binding
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- energy derivation by oxidation of organic compounds
- generation of precursor metabolites and energy
- main pathways of carbohydrate metabolism
- metabolism
- physiological process
- tricarboxylic acid cycle
|
| Component |
|
|
| Enzyme 33 General Function |
Energy production and conversion |
| Enzyme 33 Specific Function |
Not Available |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
Not Available |
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
Not Available |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
B2R545  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
B2R545_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
Not Available |
| Enzyme 33 GenBank Gene ID |
AK312056  |
| Enzyme 33 GeneCard ID |
B2R545  |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
Not Available |
| Enzyme 33 Metabolite References |
Not Available |